Ubiquitylation

Protein ubiquitylation, like phosphorylation, is a reversible post-translational modification that alters proteins in order to control intracellular signaling events. 'Ubiquitylation' or 'ubiquitination' is a process that refers to the covalent attachment of a small, 76 amino acid protein called ubiquitin to a lysine residue residing on a substrate protein that results in either monoubiquitylation or polyubiquitylation of the substrate; the latter being where chains of ubiquitin are attached to the substrate protein. Ubiquitylation is a much more complex process than phosphorylation mainly due to the ability of ubiquitin to form polyubiquitin chains of at least eight different linkage types. The structure of each chain determines whether a protein modulates a specific signaling cascade or becomes degraded (Komander. 2009).

The enzymes of the ubiquitylation pathway play a pivotal role in a number of cellular processes including the targeted proteosomal degradation of substrate proteins. Three classes of enzymes are involved in the process of ubiquitylation; activating enzymes (E1s), conjugating enzymes (E2s) and protein ligases (E3s). Ubiquitylation of substrate proteins depends on the sequential action of these three enzymes. In an ATP-dependent first step, an E1 enzyme forms a thioester linkage with ubiquitin which is then transferred onto the sulfydryl group of the active site cysteine on the E2 enzyme forming a ubiquitin-thioester intermediate. An E3, then acts as an adaptor to bind both substrate protein and E2 'loaded' with ubiquitin. The E3 facilitates isopeptide bond formation between ubiquitin and the substrate protein

Reference:

Komander D (2009) The emerging complexity of protein ubiquitination. Biochem Soc Trans 37, 937-53.


Modifiers
Ubiquigent™ Ubiquitin , Cat. No. 60-0001-010
Ubiquitin is a highly conserved protein that plays a key role in the ubiquitylation pathway. Ubiquitin is found only in eukaryotic organisms throughout which it shows strong sequence conservation (Wilkinson, 1995). The ubiquitin protein is present in all cell types and found either in free form or conjugated to proteins through a covalent bond between its C-terminal glycine and the ε-amino group of lysine residues; a process known as ubiquitination or ubiquitylation. Ubiquitylation is an essential cellular process affected by a multi-enzyme cascade involving three classes of enzyme known as activating enzymes (E1s), conjugating enzymes (E2s) and protein ligases (E3s).
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E1 Activating Enzymes
Ubiquigent™ 6His-UBA6 , Cat. No. 61-0002-010
Uba6 is a member of the E1 activating enzyme family and the human gene was first described by Jin et al. (2007). Uba6 shares 42% homology with Ube1 and contains all the structural elements required for E1 enzyme activity. Uba6 interacts with a number of E2 and E3 enzymes and has been shown to be involved with p53 ubiquitylation in vitro. Uba6 activates ubiquitin and the ubiquitin-like protein human leukocyte antigen F-Associated Transcript 10 (FAT10), both of which may serve as a signal for proteasomal degradation. Knockdown of Uba6 results in decreased FAT10 conjugation, indicating that Uba6 is required to activate FAT10 and facilitate its conjugation.
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Ubiquigent™ 6His-UBA6 , Cat. No. 61-0002-050
Uba6 is a member of the E1 activating enzyme family and the human gene was first described by Jin et al. (2007). Uba6 shares 42% homology with Ube1 and contains all the structural elements required for E1 enzyme activity. Uba6 interacts with a number of E2 and E3 enzymes and has been shown to be involved with p53 ubiquitylation in vitro. Uba6 activates ubiquitin and the ubiquitin-like protein human leukocyte antigen F-Associated Transcript 10 (FAT10), both of which may serve as a signal for proteasomal degradation. Knockdown of Uba6 results in decreased FAT10 conjugation, indicating that Uba6 is required to activate FAT10 and facilitate its conjugation.
50 μg
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Ubiquigent™ 6His-Ube1 , Cat. No. 61-0001-010
Ube1 is a member of the E1 activating enzyme family and cloning of the human gene was first described by Handley et al. (1991). Ube1 ‘activates’ ubiquitin through catalysing a C-terminal ATP dependent adenylation of the protein which results in it forming a high-energy thioester bond with the sulfhydryl group of Ube1. Ube1 is monomeric and there are two active sites within the Ube1 protein allowing it to bind two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site. Defects in Ube1 are known to cause spinal muscular atrophy X-linked type 2 (SMAX2) also known as X-linked lethal infantile spinal muscular atrophy, distal X-linked arthrogryposis multiplex congenita or X-linked arthrogryposis type 1 (AMCX1).
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Ubiquigent™ 6His-Ube1 , Cat. No. 61-0001-050
Ube1 is a member of the E1 activating enzyme family and cloning of the human gene was first described by Handley et al. (1991). Ube1 ‘activates’ ubiquitin through catalysing a C-terminal ATP dependent adenylation of the protein which results in it forming a high-energy thioester bond with the sulfhydryl group of Ube1. Ube1 is monomeric and there are two active sites within the Ube1 protein allowing it to bind two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site. Defects in Ube1 are known to cause spinal muscular atrophy X-linked type 2 (SMAX2) also known as X-linked lethal infantile spinal muscular atrophy, distal X-linked arthrogryposis multiplex congenita or X-linked arthrogryposis type 1 (AMCX1).
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E2 Conjugating Enzymes
Ubiquigent­™ GST-Ube2A , Cat. No. 62-0001-020
Ube2A is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Koken et al. (1991). Ube2A shares 70% identity with its yeast homologue but lacks the acidic C-terminal domain. The ring finger proteins RAD5 and RAD18 interact with Ube2A and other members of the RAD6 pathway. Phosphorylation of Ube2A by CDK1 and 2 increases its activity during the G2/M phase of the cell cycle. Ube2A is required for post-replicative DNA damage repair in eukaryotic cells. A nonsense mutation resulting in the loss of a 25 amino acid region in the C-terminal domain of Ube2A has been identified as a cause of a novel X-linked mental retardation (XLMR) syndrome.
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Ubiquigent­™ GST-Ube2A , Cat. No. 62-0001-100
Ube2A is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Koken et al. (1991). Ube2A shares 70% identity with its yeast homologue but lacks the acidic C-terminal domain. The ring finger proteins RAD5 and RAD18 interact with Ube2A and other members of the RAD6 pathway. Phosphorylation of Ube2A by CDK1 and 2 increases its activity during the G2/M phase of the cell cycle. Ube2A is required for post-replicative DNA damage repair in eukaryotic cells. A nonsense mutation resulting in the loss of a 25 amino acid region in the C-terminal domain of Ube2A has been identified as a cause of a novel X-linked mental retardation (XLMR) syndrome.
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Ubiquigent­™ GST-Ube2B , Cat. No. 62-0003-020
Ube2B is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Koken et al., (1991). Ube2B shares 70% identity with its yeast homologue but lacks the acidic C-terminal domain. The ring finger proteins RAD5 and RAD18 interact with Ube2B. In complex Ube2B and RAD18 trigger replication fork stalling at DNA damage sites during the post replicative repair process. Null mutations of the Ube2B gene in mice are associated with structural abnormalities in sperm and SNP analysis of human Ube2B variants has provided evidence for association of this gene with male infertility.
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Ubiquigent­™ GST-Ube2B , Cat. No. 62-0003-100
Ube2B is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Koken et al., (1991). Ube2B shares 70% identity with its yeast homologue but lacks the acidic C-terminal domain. The ring finger proteins RAD5 and RAD18 interact with Ube2B. In complex Ube2B and RAD18 trigger replication fork stalling at DNA damage sites during the post replicative repair process. Null mutations of the Ube2B gene in mice are associated with structural abnormalities in sperm and SNP analysis of human Ube2B variants has provided evidence for association of this gene with male infertility.
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Ubiquigent­™ GST-Ube2C , Cat. No. 62-0006-020
Ube2C is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Townsley et al. (1997). Ube2C shares 85% and 61% homology with frog and clam sequences respectively, and contains a 30 amino acid N-terminal extension. Ube2C binds APC11 and APC2 resulting in their autoubiquitylation and proteasomal degradation, a switch in the APC complex which causes sister chromatid separation and exit from mitosis. Ube2C has also been identified as a molecular marker useful in non small cell lung carcinoma (NSCLC) prognosis.
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Ubiquigent­™ GST-Ube2C , Cat. No. 62-0006-100
Ube2C is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Townsley et al. (1997). Ube2C shares 85% and 61% homology with frog and clam sequences respectively, and contains a 30 amino acid N-terminal extension. Ube2C binds APC11 and APC2 resulting in their autoubiquitylation and proteasomal degradation, a switch in the APC complex which causes sister chromatid separation and exit from mitosis. Ube2C has also been identified as a molecular marker useful in non small cell lung carcinoma (NSCLC) prognosis.
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Ubiquigent­™ GST-Ube2D1 , Cat. No. 62-0009-020
Ube2D1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Scheffner et al. (1994). Ube2D1 shares 89% sequence identity with its Drosophila homologue and mediates E6/UBE3A (E6AP)-induced ubiquitylation of p53. Ubiquitylation of the yeast PTS1 import receptor (pex5p) has been demonstrated in an in vitro assay in the presence of the human Ube2D1 in combination with the ring domain of the yeast E3 ligase pex10p. Sequence encoding the stimulated iron transport gene SFT overlaps with intron 7 and exon 6 of Ube2D1, and RT/PCR has shown significantly upregulated levels of Ube2D1 in livers of iron-overloaded patients with hereditary hemochromatosis.
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Ubiquigent­™ GST-Ube2D1 , Cat. No. 62-0009-100
Ube2D1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Scheffner et al. (1994). Ube2D1 shares 89% sequence identity with its Drosophila homologue and mediates E6/UBE3A (E6AP)-induced ubiquitylation of p53. Ubiquitylation of the yeast PTS1 import receptor (pex5p) has been demonstrated in an in vitro assay in the presence of the human Ube2D1 in combination with the ring domain of the yeast E3 ligase pex10p. Sequence encoding the stimulated iron transport gene SFT overlaps with intron 7 and exon 6 of Ube2D1, and RT/PCR has shown significantly upregulated levels of Ube2D1 in livers of iron-overloaded patients with hereditary hemochromatosis.
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Ubiquigent­™ GST-Ube2D2 , Cat. No. 62-0011-020
Ube2D2 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Jensen et al. (1995). Ube2D2 shares 95% and 79% sequence identity with the Drosophila and S. cerevisiae homologues respectively. Ube2D2 can conjugate ubiquitin to targets in an E6AP dependent manner. Ube2D2 forms part of a ubiquitin E3 ligase complex with Cullin1, Skp1, Roc1 and BTRC. This complex has been shown to mediate activation of NFκB and promote degradation of phosphorylated IκBα. Co-immunoprecipitation has shown that the Shigella flexneri effector protein (OspG) interacts with Ube2D2. Glial cell missing homolog 1 (GCM1) is an important transcription factor regulating placental cell fusion and it has been shown that Ube2D2 is required for Skp1-Cullin-F-Box (SCF) E3 ligase mediated ubiquitylation of GCM1. Ube2D2 also supports mdm2 mediated ubiquitylation of p53.
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Ubiquigent­™ GST-Ube2D2 , Cat. No. 62-0011-100
Ube2D2 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Jensen et al. (1995). Ube2D2 shares 95% and 79% sequence identity with the Drosophila and S. cerevisiae homologues respectively. Ube2D2 can conjugate ubiquitin to targets in an E6AP dependent manner. Ube2D2 forms part of a ubiquitin E3 ligase complex with Cullin1, Skp1, Roc1 and BTRC. This complex has been shown to mediate activation of NFκB and promote degradation of phosphorylated IκBα. Co-immunoprecipitation has shown that the Shigella flexneri effector protein (OspG) interacts with Ube2D2. Glial cell missing homolog 1 (GCM1) is an important transcription factor regulating placental cell fusion and it has been shown that Ube2D2 is required for Skp1-Cullin-F-Box (SCF) E3 ligase mediated ubiquitylation of GCM1. Ube2D2 also supports mdm2 mediated ubiquitylation of p53.
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Ubiquigent­™ GST-Ube2D3 , Cat. No. 62-0013-020
Ube2D3 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the gene was first described by Jensen et al. (1995). The E3 ligase E6AP mediates the conjugation of ubiquitin to targets such as p53 via Ube2D3. Activation of the IKK complex is mediated by unanchored polyubiquitin chains formed by Ube2D3 and TRAF6. Zipper-Interacting Protein Kinase (ZIPK) is a serine/threonine kinase implicated in cell death and transcriptional regulation, Ube2D3 induces ZIPK accumulation in promyelocytic leukaemia protein nuclear bodies resulting in their ubiquitylation. Meibomian Cell Carcinoma (MCC) is a malignant tumour of the meibomian glands located in the eyelids. Ube2D3 has been identified by RT/PCR as one of five genes found to be upregulated in MCC tumours.
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Ubiquigent­™ GST-Ube2D3 , Cat. No. 62-0013-100
Ube2D3 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the gene was first described by Jensen et al. (1995). The E3 ligase E6AP mediates the conjugation of ubiquitin to targets such as p53 via Ube2D3. Activation of the IKK complex is mediated by unanchored polyubiquitin chains formed by Ube2D3 and TRAF6. Zipper-Interacting Protein Kinase (ZIPK) is a serine/threonine kinase implicated in cell death and transcriptional regulation, Ube2D3 induces ZIPK accumulation in promyelocytic leukaemia protein nuclear bodies resulting in their ubiquitylation. Meibomian Cell Carcinoma (MCC) is a malignant tumour of the meibomian glands located in the eyelids. Ube2D3 has been identified by RT/PCR as one of five genes found to be upregulated in MCC tumours.
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Ubiquigent­™ GST-Ube2D4 , Cat. No. 62-0016-020
Ube2D4 is a member of the E2 ubiquitin-conjugating enzyme family and the human gene was first described by Colland et al. (2004).
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Ubiquigent­™ GST-Ube2D4 , Cat. No. 62-0016-100
Ube2D4 is a member of the E2 ubiquitin-conjugating enzyme family and the human gene was first described by Colland et al. (2004).
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Ubiquigent­™ GST-Ube2E1 , Cat. No. 62-0018-020
Ube2E1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Nuber et al. (1996). Ube2E1 shares 74% sequence homology with Ube2D1 and has an N-terminal extension of approximately 40 amino acids. Ube2E1 modulates the transcriptional repression activity of Ataxin-1, the gene product of Spinocerebellar ataxia type 1 (SCA1). SCA1 is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration, which is caused by expansion of the polyglutamine tract in Ataxin-1. Ataxin-1 binds with Ube2E1 through its AXH domain and in vitro the rate of Ataxin-1 degradation is regulated by Ube2E1. Ube2E1 may have some therapeutic potential in the treatment of SCA1 by modulating the degradation of Ataxin-1.
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Ubiquigent­™ GST-Ube2E1 , Cat. No. 62-0018-100
Ube2E1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Nuber et al. (1996). Ube2E1 shares 74% sequence homology with Ube2D1 and has an N-terminal extension of approximately 40 amino acids. Ube2E1 modulates the transcriptional repression activity of Ataxin-1, the gene product of Spinocerebellar ataxia type 1 (SCA1). SCA1 is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration, which is caused by expansion of the polyglutamine tract in Ataxin-1. Ataxin-1 binds with Ube2E1 through its AXH domain and in vitro the rate of Ataxin-1 degradation is regulated by Ube2E1. Ube2E1 may have some therapeutic potential in the treatment of SCA1 by modulating the degradation of Ataxin-1.
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Ubiquigent­™ GST-Ube2E3 , Cat. No. 62-0021-020
Ube2E3 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the gene was first described by Ito et al (1999). Ube2E3 binds to the RING-finger proteins ARA54 and RNF8, thought to act as E3 ligases in the ubiquitylation of nuclear proteins. The epithelial Na+ channel (ENaC) is regulated by Ube2E3 and the E3 ligase NEDD4.2. Ube2E3 interacts with NEDD4.2 via its UBC domain and ubiquitylation of ENaC occurs by NEDD4.2 binding the PY motifs of its α, β and γ subunits. NEDD4.2 is a negative regulator of ENaC and deletions in the PY motifs of the β and γ subunits of ENaC cause Liddle’s syndrome, an inherited form of hypertension. The loss of NEDD4.2 binding sites in mutated ENaC causes an increase in channel number at the cell surface and increased Na+ reabsorption by the distal nephron, resulting in hypertension.
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Ubiquigent­™ GST-Ube2E3 , Cat. No. 62-0021-100
Ube2E3 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the gene was first described by Ito et al (1999). Ube2E3 binds to the RING-finger proteins ARA54 and RNF8, thought to act as E3 ligases in the ubiquitylation of nuclear proteins. The epithelial Na+ channel (ENaC) is regulated by Ube2E3 and the E3 ligase NEDD4.2. Ube2E3 interacts with NEDD4.2 via its UBC domain and ubiquitylation of ENaC occurs by NEDD4.2 binding the PY motifs of its α, β and γ subunits. NEDD4.2 is a negative regulator of ENaC and deletions in the PY motifs of the β and γ subunits of ENaC cause Liddle’s syndrome, an inherited form of hypertension. The loss of NEDD4.2 binding sites in mutated ENaC causes an increase in channel number at the cell surface and increased Na+ reabsorption by the distal nephron, resulting in hypertension.
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Ubiquigent­™ GST-Ube2F , Cat. No. 62-0024-020
Ube2F is a member of the ubiquitin-like E2 conjugating enzyme family and the human gene was first described by Huang et al. (2009). Ube2F acts as a NEDD8 conjugating enzyme both in vitro and in vivo. Ube2F accepts the ubiquitin-like protein NEDD8 from the Uba3-NAE1 (APP-BP1/Uba3) E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction of Ube2F with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-Ube2F complex NEDDylates specific target proteins such as CUL5, a component of one of the many Cullin Ring Ligases (CRLs).
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Ubiquigent­™ GST-Ube2F , Cat. No. 62-0024-100
Ube2F is a member of the ubiquitin-like E2 conjugating enzyme family and the human gene was first described by Huang et al. (2009). Ube2F acts as a NEDD8 conjugating enzyme both in vitro and in vivo. Ube2F accepts the ubiquitin-like protein NEDD8 from the Uba3-NAE1 (APP-BP1/Uba3) E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction of Ube2F with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-Ube2F complex NEDDylates specific target proteins such as CUL5, a component of one of the many Cullin Ring Ligases (CRLs).
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Ubiquigent­™ GST-Ube2G1 , Cat. No. 62-0027-020
Ube2G1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Watanabe et al. (1996). Ube2G1 shares 74% sequence identity with UBC7 from C. elegans and a high degree of homology with UBC7 from other species. Expression of Ube2G1 and a helix-loop-helix transcription factor and member of the MYC/MAX superfamily (ROX/MNT) is decreased in medullablastoma tumours. Haploid sufficiency of the human 17p13.3 region is associated with 35% to 50% of medulloblastomas, indicating the presence of one or more tumour suppressor genes which have not yet been identified.
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Ubiquigent­™ GST-Ube2G1 , Cat. No. 62-0027-100
Ube2G1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Watanabe et al. (1996). Ube2G1 shares 74% sequence identity with UBC7 from C. elegans and a high degree of homology with UBC7 from other species. Expression of Ube2G1 and a helix-loop-helix transcription factor and member of the MYC/MAX superfamily (ROX/MNT) is decreased in medullablastoma tumours. Haploid sufficiency of the human 17p13.3 region is associated with 35% to 50% of medulloblastomas, indicating the presence of one or more tumour suppressor genes which have not yet been identified.
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Ubiquigent­™ GST-Ube2G2 , Cat. No. 62-0029-020
Ube2G2 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Katsanis and Fischer (1998). The Ube2G2 gene encodes a 165-amino-acid protein that shares 57% sequence identity with Ube2G1. Ube2G2 is involved in protein degradation, including a process known as Endoplasmic Reticulum-Associated Degradation (ERAD). Ube2G2 binds the E3 ligase GP78 and the affinity of this interaction is significantly increased by the G2BR domain on GP78. The Ube2G2/GP78 interaction results in the preassembly of Lys-48-linked ubiquitin chains on the catalytic cysteine of Ube2G2. A C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum - TEB4 – also catalyses Lys-48-linked polyubiquitylation employing Ube2G2 in vitro.
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Ubiquigent­™ GST-Ube2G2 , Cat. No. 62-0029-100
Ube2G2 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Katsanis and Fischer (1998). The Ube2G2 gene encodes a 165-amino-acid protein that shares 57% sequence identity with Ube2G1. Ube2G2 is involved in protein degradation, including a process known as Endoplasmic Reticulum-Associated Degradation (ERAD). Ube2G2 binds the E3 ligase GP78 and the affinity of this interaction is significantly increased by the G2BR domain on GP78. The Ube2G2/GP78 interaction results in the preassembly of Lys-48-linked ubiquitin chains on the catalytic cysteine of Ube2G2. A C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum - TEB4 – also catalyses Lys-48-linked polyubiquitylation employing Ube2G2 in vitro.
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Ubiquigent­™ GST-Ube2H , Cat. No. 62-0031-020
Ube2H is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Kaiser et al. (1994). Human Ube2H shares 54% identity with the yeast homologue (UbcH8) and full length forms of both the human and yeast enzymes showed similar enzymatic activities in vitro by catalyzing the ubiquitylation of histones. Ube2H has been mapped to a region on chromosome 7 and the gene has been identified as a candidate for involvement in an autistic disorder with neurodevelopmental complications. An association has also been made between Ube2H and the motor neuron disorder amyotrophic lateral sclerosis (ALS) where single strand conformation polymorphism (SSCP) analysis identified a known and sporadic polymorphism in the gene.
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Ubiquigent­™ GST-Ube2H , Cat. No. 62-0031-100
Ube2H is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Kaiser et al. (1994). Human Ube2H shares 54% identity with the yeast homologue (UbcH8) and full length forms of both the human and yeast enzymes showed similar enzymatic activities in vitro by catalyzing the ubiquitylation of histones. Ube2H has been mapped to a region on chromosome 7 and the gene has been identified as a candidate for involvement in an autistic disorder with neurodevelopmental complications. An association has also been made between Ube2H and the motor neuron disorder amyotrophic lateral sclerosis (ALS) where single strand conformation polymorphism (SSCP) analysis identified a known and sporadic polymorphism in the gene.
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Ubiquigent­™ GST-Ube2I , Cat. No. 62-0065-020
Ube2I is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Wang et al. (1996). The candidate tumour suppressor gene Fragile Histidine Triad (FHIT) located on 3p14.2 is deleted in many types of human cancer. Ube2I binds to FHIT and this interaction is thought to be involved in the degradation of S and M phase cyclins and cell cycle control. Proliferating Cell Nuclear Antigen (PCNA) a DNA polymerase sliding clamp involved in DNA synthesis and repair is a substrate for Ube2I. SUMOylation of Amyloid Precursor Protein (APP) is reported to be associated with decreased levels of beta amyloid (Abeta) aggregates, suggesting a role in the pathogenesis of Alzheimer’s Disease (AD). An investigation into single nucleotide polymorphisms (SNPs) in the Ube2I gene has shown an association between this and the risk of late onset AD.
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Ubiquigent­™ GST-Ube2I , Cat. No. 62-0065-100
Ube2I is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Wang et al. (1996). The candidate tumour suppressor gene Fragile Histidine Triad (FHIT) located on 3p14.2 is deleted in many types of human cancer. Ube2I binds to FHIT and this interaction is thought to be involved in the degradation of S and M phase cyclins and cell cycle control. Proliferating Cell Nuclear Antigen (PCNA) a DNA polymerase sliding clamp involved in DNA synthesis and repair is a substrate for Ube2I. SUMOylation of Amyloid Precursor Protein (APP) is reported to be associated with decreased levels of beta amyloid (Abeta) aggregates, suggesting a role in the pathogenesis of Alzheimer’s Disease (AD). An investigation into single nucleotide polymorphisms (SNPs) in the Ube2I gene has shown an association between this and the risk of late onset AD.
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Ubiquigent­™ GST-Ube2K , Cat. No. 62-0038-020
Ube2K is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Kalchman et al. (1996). Interaction and selective binding of Ube2K to the N-terminus of huntingtin, the causal gene product in Huntington’s disease has been demonstrated. Ube2K directs the synthesis of Lys63- or Lys48-linked ubiquitin chains on BRCA1. Ube2K was identified in a screen for novel SUMO targets, however attachment of SUMO to Ube2K in vitro severely impairs ubiquitin thioester and unanchored ubiquitin chain formation. The ubiquitin-proteasome system malfunction in Alzheimer’s disease (AD) has been attributed to neurotoxicity and proteasome inhibition by Abeta, which is mediated by an increase in the levels of Ube2K found in the brains of patients with AD.
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Ubiquigent­™ GST-Ube2K , Cat. No. 62-0038-100
Ube2K is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Kalchman et al. (1996). Interaction and selective binding of Ube2K to the N-terminus of huntingtin, the causal gene product in Huntington’s disease has been demonstrated. Ube2K directs the synthesis of Lys63- or Lys48-linked ubiquitin chains on BRCA1. Ube2K was identified in a screen for novel SUMO targets, however attachment of SUMO to Ube2K in vitro severely impairs ubiquitin thioester and unanchored ubiquitin chain formation. The ubiquitin-proteasome system malfunction in Alzheimer’s disease (AD) has been attributed to neurotoxicity and proteasome inhibition by Abeta, which is mediated by an increase in the levels of Ube2K found in the brains of patients with AD.
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Ubiquigent­™ GST-Ube2L3 , Cat. No. 62-0041-020
Ube2L3 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Moynihan et al. (1998). A protein complex comprising Ube2L3, the E3 ligase Parkin and alpha synuclein (alpha-Sp22) has been identified in which the substrate alpha-Sp22 becomes polyubiquitylated in normal human brains and targeted for degradation. Loss of Parkin function causes pathologic accumulation of alpha-Sp22 in the brain which is associated with Parkinson’s disease. Changes in levels of Ube2L3 during the cell cycle regulate entrance into and progression through S phase. Ube2L3 levels decrease during S-phase but are restored in G2, it is thought progression into G2 occurs by Ube2L3 modulation of the intra-S phase checkpoint mediated by Chk1.
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Ubiquigent­™ GST-Ube2L3 , Cat. No. 62-0041-100
Ube2L3 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Moynihan et al. (1998). A protein complex comprising Ube2L3, the E3 ligase Parkin and alpha synuclein (alpha-Sp22) has been identified in which the substrate alpha-Sp22 becomes polyubiquitylated in normal human brains and targeted for degradation. Loss of Parkin function causes pathologic accumulation of alpha-Sp22 in the brain which is associated with Parkinson’s disease. Changes in levels of Ube2L3 during the cell cycle regulate entrance into and progression through S phase. Ube2L3 levels decrease during S-phase but are restored in G2, it is thought progression into G2 occurs by Ube2L3 modulation of the intra-S phase checkpoint mediated by Chk1.
100 μg
$199.00
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Ubiquigent­™ GST-Ube2N , Cat. No. 62-0046-020
Ube2N is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Yamaguchi et al. (1996). In yeast, Ube2N forms a specific heteromeric complex with MMS2 a signaling component of the RAD6 pathway. Cytokine receptor signaling results in complex formation of protein kinases such as CD40 with TRAF2 and TRAF3, Ube2N, cellular inhibitor of apoptosis protein-1 (CIAP1) and -2 (CIAP2), IKK-α and MEKK1. Translocation of a TRAF2, Ube2N, and IKK-α complex from the membrane to the cytosol is initiated by a CIAP1/CIAP2-induced degradation of TRAF3 which results in activation of MEKK1 and MAP kinase cascades. Heterozygous Ube2N mice exhibit selectively impaired activation of signal transduction pathways initiated by TNFr and show reduced ubiquitylation of TRAF6. Reducing Ube2N activity may have therapeutic uses in controlling inflammatory responses.
20 μg
$99.00
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Ubiquigent­™ GST-Ube2N , Cat. No. 62-0046-100
Ube2N is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Yamaguchi et al. (1996). In yeast, Ube2N forms a specific heteromeric complex with MMS2 a signaling component of the RAD6 pathway. Cytokine receptor signaling results in complex formation of protein kinases such as CD40 with TRAF2 and TRAF3, Ube2N, cellular inhibitor of apoptosis protein-1 (CIAP1) and -2 (CIAP2), IKK-α and MEKK1. Translocation of a TRAF2, Ube2N, and IKK-α complex from the membrane to the cytosol is initiated by a CIAP1/CIAP2-induced degradation of TRAF3 which results in activation of MEKK1 and MAP kinase cascades. Heterozygous Ube2N mice exhibit selectively impaired activation of signal transduction pathways initiated by TNFr and show reduced ubiquitylation of TRAF6. Reducing Ube2N activity may have therapeutic uses in controlling inflammatory responses.
100 μg
$199.00
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Ubiquigent­™ GST-Ube2Q , Cat. No. 62-0049-020
Ube2Q is a member of the E2 conjugating enzyme family. Cloning of human Ube2Q was first described by Marenholz et al. in 2001. Ube2Q shares 50-75% sequence identity to its homologues in Mus musculus, Drosophila, C. elegans and Xenopus. Murine Ube2Q has a conserved sequence for ubiquitin binding shared by all the ubiquitin-conjugating enzymes and its NH2-terminal domain appears critical for the binding and internalization of cell surface galactosyltransferase 1 (GalT1) in embryonic stem cells. Ube2Q regulates GalT1-associated laminin-dependent embryonic cell adhesion and the formation of embryoid bodies.
20 μg
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Ubiquigent­™ GST-Ube2Q , Cat. No. 62-0049-100
Ube2Q is a member of the E2 conjugating enzyme family. Cloning of human Ube2Q was first described by Marenholz et al. in 2001. Ube2Q shares 50-75% sequence identity to its homologues in Mus musculus, Drosophila, C. elegans and Xenopus. Murine Ube2Q has a conserved sequence for ubiquitin binding shared by all the ubiquitin-conjugating enzymes and its NH2-terminal domain appears critical for the binding and internalization of cell surface galactosyltransferase 1 (GalT1) in embryonic stem cells. Ube2Q regulates GalT1-associated laminin-dependent embryonic cell adhesion and the formation of embryoid bodies.
100 μg
$199.00
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Ubiquigent­™ GST-Ube2R1 , Cat. No. 62-0053-020
Ube2R1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Plon et al. in 1993. Casein Kinase type II (CK2) mediated phosphorylation of Ube2R1 increases ubiquitylation of Sic-1 in the presence of the E3 ligase S-phase kinase-associated protein 1/Cullin/F-box/Cdc4 (SCFCdc4) during cell cycle progression. Specific binding of CK2 phosphorylated Ube2R1 to beta-TRCP (β-TRCP) - the substrate recognition unit of the SCF ligase - enhances degradation of its substrate beta-catenin. Ube2R1 also catalyzes polyubiquitylation of a substrate recruited by the Skp1-Cullin 1-F-box protein-ROC1 E3 ubiquitin ligase. Downregulation of Ube2R1 following let-7 overexpression in primary fibroblasts results in reduced SCF activity, stabilization of the Wee1 kinase, and an increased fraction of the cells in G(2)/M.
20 μg
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Ubiquigent­™ GST-Ube2R1 , Cat. No. 62-0053-100
Ube2R1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Plon et al. in 1993. Casein Kinase type II (CK2) mediated phosphorylation of Ube2R1 increases ubiquitylation of Sic-1 in the presence of the E3 ligase S-phase kinase-associated protein 1/Cullin/F-box/Cdc4 (SCFCdc4) during cell cycle progression. Specific binding of CK2 phosphorylated Ube2R1 to beta-TRCP (β-TRCP) - the substrate recognition unit of the SCF ligase - enhances degradation of its substrate beta-catenin. Ube2R1 also catalyzes polyubiquitylation of a substrate recruited by the Skp1-Cullin 1-F-box protein-ROC1 E3 ubiquitin ligase. Downregulation of Ube2R1 following let-7 overexpression in primary fibroblasts results in reduced SCF activity, stabilization of the Wee1 kinase, and an increased fraction of the cells in G(2)/M.
100 μg
$199.00
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Ubiquigent­™ GST-Ube2S , Cat. No. 62-0055-020
Ube2S is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Liu et al. in 1992. The tumour suppressor protein Von Hippel-Lindau (VHL) associates with and is targeted by Ube2S for ubiquitin-mediated proteolysis in human cell lines. Over expression of Ube2S increases tumour cell proliferation, invasion, and metastasis through the VHL-HIF pathway and has been found to correlate positively with HIF-1A in tumour cell line. Ube2S can elongate ubiquitin chains initiated by the E2 enzymes Ube2C and Ube2D1, enhancing the degradation of APC/C substrates by the proteasome. Recently Ube2S has been shown to assemble K11-specific chains for human and Drosophila APC/C. Chain specific activity of Ube2S is dependent on cell cycle-dependent association with the APC/C activators Cdc20 and Cdh1. Depletion of Ube2S has been shown to result in severe spindle defects and mitotic delay.
20 μg
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Ubiquigent­™ GST-Ube2S , Cat. No. 62-0055-100
Ube2S is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Liu et al. in 1992. The tumour suppressor protein Von Hippel-Lindau (VHL) associates with and is targeted by Ube2S for ubiquitin-mediated proteolysis in human cell lines. Over expression of Ube2S increases tumour cell proliferation, invasion, and metastasis through the VHL-HIF pathway and has been found to correlate positively with HIF-1A in tumour cell line. Ube2S can elongate ubiquitin chains initiated by the E2 enzymes Ube2C and Ube2D1, enhancing the degradation of APC/C substrates by the proteasome. Recently Ube2S has been shown to assemble K11-specific chains for human and Drosophila APC/C. Chain specific activity of Ube2S is dependent on cell cycle-dependent association with the APC/C activators Cdc20 and Cdh1. Depletion of Ube2S has been shown to result in severe spindle defects and mitotic delay.
100 μg
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Ubiquigent™ 6His-Ube2C , Cat. No. 62-0005-020
Ube2C is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Townsley et al. (1997). Ube2C shares 85% and 61% homology with frog and clam sequences respectively, and contains a 30 amino acid N-terminal extension. Ube2C binds APC11 and APC2 resulting in their autoubiquitylation and proteasomal degradation, a switch in the APC complex which causes sister chromatid separation and exit from mitosis. Ube2C has also been identified as a molecular marker useful in non small cell lung carcinoma (NSCLC) prognosis.
20 μg
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Ubiquigent™ 6His-Ube2C , Cat. No. 62-0005-100
Ube2C is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Townsley et al. (1997). Ube2C shares 85% and 61% homology with frog and clam sequences respectively, and contains a 30 amino acid N-terminal extension. Ube2C binds APC11 and APC2 resulting in their autoubiquitylation and proteasomal degradation, a switch in the APC complex which causes sister chromatid separation and exit from mitosis. Ube2C has also been identified as a molecular marker useful in non small cell lung carcinoma (NSCLC) prognosis.
100 μg
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Ubiquigent™ 6His-Ube2D1 , Cat. No. 62-0008-020
Ube2D1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Scheffner et al. (1994). Ube2D1 shares 89% sequence identity with its Drosophila homologue and mediates E6/UBE3A (E6AP)-induced ubiquitylation of p53. Ubiquitylation of the yeast PTS1 import receptor (pex5p) has been demonstrated in an in vitro assay in the presence of the human Ube2D1 in combination with the ring domain of the yeast E3 ligase pex10p. Sequence encoding the stimulated Iron transport gene SFT overlaps with intron 7 and exon 6 of Ube2D1, and RT/PCR has shown significantly upregulated levels of Ube2D1 in livers of iron-overloaded patients with hereditary hemochromatosis.
20 μg
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Ubiquigent™ 6His-Ube2D1 , Cat. No. 62-0008-100
Ube2D1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Scheffner et al. (1994). Ube2D1 shares 89% sequence identity with its Drosophila homologue and mediates E6/UBE3A (E6AP)-induced ubiquitylation of p53. Ubiquitylation of the yeast PTS1 import receptor (pex5p) has been demonstrated in an in vitro assay in the presence of the human Ube2D1 in combination with the ring domain of the yeast E3 ligase pex10p. Sequence encoding the stimulated Iron transport gene SFT overlaps with intron 7 and exon 6 of Ube2D1, and RT/PCR has shown significantly upregulated levels of Ube2D1 in livers of iron-overloaded patients with hereditary hemochromatosis.
100 μg
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Ubiquigent™ 6His-Ube2D4 , Cat. No. 62-0015-020
Ube2D4 is a member of the E2 ubiquitin-conjugating enzyme family and the human gene was first described by Colland et al. (2004).
20 μg
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Ubiquigent™ 6His-Ube2D4 , Cat. No. 62-0015-100
Ube2D4 is a member of the E2 ubiquitin-conjugating enzyme family and the human gene was first described by Colland et al. (2004).
100 μg
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Ubiquigent™ 6His-Ube2E2 , Cat. No. 62-0020-020
Ube2E2 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Kimura et al. (1997). The Ubc domain of Ube2E2 shares over 90% identity with human Ube2E1, mouse UbcM2, and Drosophila UbcD2. Ube2E2 has been shown to ubiquitylate the E3 ligase E6AP by binding to its HECT domain. A yeast two hybrid screen identified two Ube2E2 binding proteins, UbcH7-Associated Protein (H7-AP1) and Human Homologue of Drosophila ARIadne (HHARI); both of these proteins are characterized by the presence of a RING finger and In Between RING finger (IBR) domains. Ube2E2 has also been shown to bind the ubiquitin-protein ligase Parkin via its C-terminal ring-finger domain, resulting in ubiquitylation of the synaptic vesicle associated protein CDCrel-1.
20 μg
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Ubiquigent™ 6His-Ube2E2 , Cat. No. 62-0020-100
Ube2E2 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Kimura et al. (1997). The Ubc domain of Ube2E2 shares over 90% identity with human Ube2E1, mouse UbcM2, and Drosophila UbcD2. Ube2E2 has been shown to ubiquitylate the E3 ligase E6AP by binding to its HECT domain. A yeast two hybrid screen identified two Ube2E2 binding proteins, UbcH7-Associated Protein (H7-AP1) and Human Homologue of Drosophila ARIadne (HHARI); both of these proteins are characterized by the presence of a RING finger and In Between RING finger (IBR) domains. Ube2E2 has also been shown to bind the ubiquitin-protein ligase Parkin via its C-terminal ring-finger domain, resulting in ubiquitylation of the synaptic vesicle associated protein CDCrel-1.
100 μg
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Ubiquigent™ 6His-Ube2F , Cat. No. 62-0023-020
Ube2F is a member of the ubiquitin-like E2 conjugating enzyme family and the human gene was first described by Huang et al. (2009). Ube2F acts as a NEDD8 conjugating enzyme both in vitro and in vivo. Ube2F accepts the ubiquitin-like protein NEDD8 from the Uba3-NAE1 (APP-BP1/Uba3) E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction of Ube2F with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-Ube2F complex NEDDylates specific target proteins such as CUL5, a component of one of the many Cullin Ring Ligases (CRLs).
20 μg
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Ubiquigent™ 6His-Ube2F , Cat. No. 62-0023-100
Ube2F is a member of the ubiquitin-like E2 conjugating enzyme family and the human gene was first described by Huang et al. (2009). Ube2F acts as a NEDD8 conjugating enzyme both in vitro and in vivo. Ube2F accepts the ubiquitin-like protein NEDD8 from the Uba3-NAE1 (APP-BP1/Uba3) E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction of Ube2F with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-Ube2F complex NEDDylates specific target proteins such as CUL5, a component of one of the many Cullin Ring Ligases (CRLs).
100 μg
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Ubiquigent™ 6His-Ube2G1 , Cat. No. 62-0026-020
Ube2G1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Watanabe et al. (1996). Ube2G1 shares 74% sequence identity with UBC7 from C. elegans and a high degree of homology with UBC7 from other species. Expression of Ube2G1 and a helix-loop-helix transcription factor and member of the MYC/MAX superfamily (ROX/MNT) is decreased in medullablastoma tumours. Haploid sufficiency of the human 17p13.3 region is associated with 35% to 50% of medulloblastomas, indicating the presence of one or more tumour suppressor genes which have not yet been identified.
20 μg
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Ubiquigent™ 6His-Ube2G1 , Cat. No. 62-0026-100
Ube2G1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Watanabe et al. (1996). Ube2G1 shares 74% sequence identity with UBC7 from C. elegans and a high degree of homology with UBC7 from other species. Expression of Ube2G1 and a helix-loop-helix transcription factor and member of the MYC/MAX superfamily (ROX/MNT) is decreased in medullablastoma tumours. Haploid sufficiency of the human 17p13.3 region is associated with 35% to 50% of medulloblastomas, indicating the presence of one or more tumour suppressor genes which have not yet been identified.
100 μg
$199.00
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Ubiquigent™ 6His-Ube2I , Cat. No. 62-0033-020
Ube2I is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Wang et al. (1996). The candidate tumour suppressor gene Fragile Histidine Triad (FHIT) located on 3p14.2 is deleted in many types of human cancer. Ube2I binds to FHIT and this interaction is thought to be involved in the degradation of S and M phase cyclins and cell cycle control. Proliferating Cell Nuclear Antigen (PCNA) a DNA polymerase sliding clamp involved in DNA synthesis and repair is a substrate for Ube2I. SUMOylation of Amyloid Precursor Protein (APP) is reported to be associated with decreased levels of beta amyloid (Abeta) aggregates, suggesting a role in the pathogenesis of Alzheimer’s Disease (AD). An investigation into single nucleotide polymorphisms (SNPs) in the Ube2I gene has shown an association between this and the risk of late onset AD.
20 μg
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Ubiquigent™ 6His-Ube2I , Cat. No. 62-0033-100
Ube2I is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Wang et al. (1996). The candidate tumour suppressor gene Fragile Histidine Triad (FHIT) located on 3p14.2 is deleted in many types of human cancer. Ube2I binds to FHIT and this interaction is thought to be involved in the degradation of S and M phase cyclins and cell cycle control. Proliferating Cell Nuclear Antigen (PCNA) a DNA polymerase sliding clamp involved in DNA synthesis and repair is a substrate for Ube2I. SUMOylation of Amyloid Precursor Protein (APP) is reported to be associated with decreased levels of beta amyloid (Abeta) aggregates, suggesting a role in the pathogenesis of Alzheimer’s Disease (AD). An investigation into single nucleotide polymorphisms (SNPs) in the Ube2I gene has shown an association between this and the risk of late onset AD.
100 μg
$199.00
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Ubiquigent™ 6His-Ube2L3 , Cat. No. 62-0040-020
Ube2L3 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Moynihan et al. (1996). A protein complex comprising Ube2L3, the E3 ligase Parkin and alpha synuclein (alpha-Sp22) has been identified in which the substrate alpha-Sp22 becomes polyubiquitylated in normal human brains and targeted for degradation. Loss of Parkin function causes pathologic accumulation of alpha-Sp22 in the brain which is associated with Parkinson’s disease. Changes in levels of Ube2L3 during the cell cycle regulate entrance into and progression through S phase. Ube2L3 levels decrease during S-phase but are restored in G2, it is thought progression into G2 occurs by Ube2L3 modulation of the intra-S phase checkpoint mediated by Chk1.
20 μg
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Ubiquigent™ 6His-Ube2L3 , Cat. No. 62-0040-100
Ube2L3 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Moynihan et al. (1996). A protein complex comprising Ube2L3, the E3 ligase Parkin and alpha synuclein (alpha-Sp22) has been identified in which the substrate alpha-Sp22 becomes polyubiquitylated in normal human brains and targeted for degradation. Loss of Parkin function causes pathologic accumulation of alpha-Sp22 in the brain which is associated with Parkinson’s disease. Changes in levels of Ube2L3 during the cell cycle regulate entrance into and progression through S phase. Ube2L3 levels decrease during S-phase but are restored in G2, it is thought progression into G2 occurs by Ube2L3 modulation of the intra-S phase checkpoint mediated by Chk1.
100 μg
$199.00
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Ubiquigent™ 6His-Ube2N , Cat. No. 62-0045-020
Ube2N is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Yamaguchi et al. (1996). In yeast, Ube2N forms a specific heteromeric complex with MMS2 a signaling component of the RAD6 pathway. Cytokine receptor signaling results in complex formation of protein kinases such as CD40 with TRAF2 and TRAF3, Ube2N, cellular inhibitor of apoptosis protein-1 (CIAP1) and -2 (CIAP2), IKK-α and MEKK1. Translocation of a TRAF2, Ube2N, and IKK-α complex from the membrane to the cytosol is initiated by a CIAP1/CIAP2-induced degradation of TRAF3 which results in activation of MEKK1 and MAP kinase cascades. Heterozygous Ube2N mice exhibit selectively impaired activation of signal transduction pathways initiated by TNF-α and show reduced ubiquitylation of TRAF6. Reducing Ube2N activity may have therapeutic uses in controlling inflammatory responses.
20 μg
$99.00
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Ubiquigent™ 6His-Ube2N , Cat. No. 62-0045-100
Ube2N is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Yamaguchi et al. (1996). In yeast, Ube2N forms a specific heteromeric complex with MMS2 a signaling component of the RAD6 pathway. Cytokine receptor signaling results in complex formation of protein kinases such as CD40 with TRAF2 and TRAF3, Ube2N, cellular inhibitor of apoptosis protein-1 (CIAP1) and -2 (CIAP2), IKK-α and MEKK1. Translocation of a TRAF2, Ube2N, and IKK-α complex from the membrane to the cytosol is initiated by a CIAP1/CIAP2-induced degradation of TRAF3 which results in activation of MEKK1 and MAP kinase cascades. Heterozygous Ube2N mice exhibit selectively impaired activation of signal transduction pathways initiated by TNF-α and show reduced ubiquitylation of TRAF6. Reducing Ube2N activity may have therapeutic uses in controlling inflammatory responses.
100 μg
$199.00
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Ubiquigent™ 6His-Ube2Q2 , Cat. No. 62-0051-020
Ube2Q2 is a member of the E2 conjugating enzyme family. The cloning of human Ube2Q2 was first described by Crawford and Piwnica-Worms. (2001). Ube2Q2 has been found to be up-regulated in 85% of head and neck squamous cell carcinoma tumours, with an increase of 2.4-fold compared to normal tissue. Ube2Q2 has been identified as a novel oncosuppressor that inhibits tumour growth and it is thought it could function as a novel diagnostic tool and potential therapeutic target for head and neck squamous cell carcinoma. Inhibition of Ube2Q2 following treatment of HeLa cells with Microtubule Inhibiting Agent (MIA) causes mitotic arrest and increased cytotoxicity, effects only observed in the absence of MIA suggesting Ube2Q2 is only involved in this response rather than having a more general role in mitosis.
20 μg
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Ubiquigent™ 6His-Ube2Q2 , Cat. No. 62-0051-100
Ube2Q2 is a member of the E2 conjugating enzyme family. The cloning of human Ube2Q2 was first described by Crawford and Piwnica-Worms, (2001). Ube2Q2 has been found to be up-regulated in 85% of head and neck squamous cell carcinoma tumours, with an increase of 2.4-fold compared to normal tissue. Ube2Q2 has been identified as a novel oncosuppressor that inhibits tumour growth and it is thought it could function as a novel diagnostic tool and potential therapeutic target for head and neck squamous cell carcinoma. Inhibition of Ube2Q2 following treatment of HeLa cells with Microtubule Inhibiting Agent (MIA) causes mitotic arrest and increased cytotoxicity, effects only observed in the absence of MIA suggesting Ube2Q2 is only involved in this response rather than having a more general role in mitosis.
100 μg
$199.00
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Ubiquigent™ 6His-Ube2R1 , Cat. No. 62-0052-020
Ube2R1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Plon et al. (1993). Casein Kinase type II (CK2) mediated phosphorylation of Ube2R1 increases ubiquitylation of Sic-1 in the presence of the E3 ligase S-phase kinase-associated protein 1/Cullin/F-box/Cdc4 (SCFCdc4) during cell cycle progression. Specific binding of CK2 phosphorylated Ube2R1 to beta-TRCP (β-TRCP) - the substrate recognition unit of the SCF ligase - enhances degradation of its substrate beta-catenin. Ube2R1 also catalyzes polyubiquitylation of a substrate recruited by the Skp1-Cullin 1-F-box protein-ROC1 E3 ubiquitin ligase. Downregulation of Ube2R1 following let-7 overexpression in primary fibroblasts results in reduced SCF activity, stabilization of the Wee1 kinase, and an increased fraction of the cells in G(2)/M.
20 μg
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Ubiquigent™ 6His-Ube2R1 , Cat. No. 62-0052-100
Ube2R1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Plon et al. (1993). Casein Kinase type II (CK2) mediated phosphorylation of Ube2R1 increases ubiquitylation of Sic-1 in the presence of the E3 ligase S-phase kinase-associated protein 1/Cullin/F-box/Cdc4 (SCFCdc4) during cell cycle progression. Specific binding of CK2 phosphorylated Ube2R1 to beta-TRCP (β-TRCP) - the substrate recognition unit of the SCF ligase - enhances degradation of its substrate beta-catenin. Ube2R1 also catalyzes polyubiquitylation of a substrate recruited by the Skp1-Cullin 1-F-box protein-ROC1 E3 ubiquitin ligase. Downregulation of Ube2R1 following let-7 overexpression in primary fibroblasts results in reduced SCF activity, stabilization of the Wee1 kinase, and an increased fraction of the cells in G(2)/M.
100 μg
$199.00
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Ubiquigent™ 6His-Ube2T , Cat. No. 62-0057-020
Ube2T is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Zhang et al. in 2000. Ube2T is integral to the Fanconi Anemia (FA) pathway for DNA damage repair. Ube2T binds to the C-terminal PH domain of FANCL the ubiquitin ligase subunit of the FA core complex, which leads to the monoubiquitylation of FANCD2 and FANCI. E3 ligase activity is not determined by assembly of the FA core complex but by the DNA damage-induced subcellular localization of the complex to chromatin. Ube2T and FANCD2 access this subcellular fraction independently and FANCD2 monoubiquitylation is regulated by the formation of an E2/E3 holoenzyme on chromatin. Ube2T expression has been analysed in lung cancer tissue and compared to normal human tissue. Ube2T was found to be significantly upregulated at both the protein and mRNA level suggesting involvement in the malignant cell phenotype.
20 μg
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Ubiquigent™ 6His-Ube2T , Cat. No. 62-0057-100
Ube2T is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Zhang et al. in 2000. Ube2T is integral to the Fanconi Anemia (FA) pathway for DNA damage repair. Ube2T binds to the C-terminal PH domain of FANCL the ubiquitin ligase subunit of the FA core complex, which leads to the monoubiquitylation of FANCD2 and FANCI. E3 ligase activity is not determined by assembly of the FA core complex but by the DNA damage-induced subcellular localization of the complex to chromatin. Ube2T and FANCD2 access this subcellular fraction independently and FANCD2 monoubiquitylation is regulated by the formation of an E2/E3 holoenzyme on chromatin. Ube2T expression has been analysed in lung cancer tissue and compared to normal human tissue. Ube2T was found to be significantly upregulated at both the protein and mRNA level suggesting involvement in the malignant cell phenotype.
100 μg
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Ubiquigent™ Ube2A , Cat. No. 62-0002-020
Ube2A is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Koken et al. (1991). Ube2A shares 70% identity with its yeast homologue but lacks the acidic C-terminal domain. The ring finger proteins RAD5 and RAD18 interact with Ube2A and other members of the RAD6 pathway. Phosphorylation of Ube2A by CDK1 and 2 increases its activity during the G2/M phase of the cell cycle. Ube2A is required for post-replicative DNA damage repair in eukaryotic cells and it is thought binding to ZNF198 may be involved in this process. A nonsense mutation resulting in the loss of a 25 amino acid region in the C-terminal domain of Ube2A has been identified as a cause of a novel X-linked mental retardation (XLMR) syndrome.
20 μg
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Ubiquigent™ Ube2A , Cat. No. 62-0002-100
Ube2A is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Koken et al. (1991). Ube2A shares 70% identity with its yeast homologue but lacks the acidic C-terminal domain. The ring finger proteins RAD5 and RAD18 interact with Ube2A and other members of the RAD6 pathway. Phosphorylation of Ube2A by CDK1 and 2 increases its activity during the G2/M phase of the cell cycle. Ube2A is required for post-replicative DNA damage repair in eukaryotic cells and it is thought binding to ZNF198 may be involved in this process. A nonsense mutation resulting in the loss of a 25 amino acid region in the C-terminal domain of Ube2A has been identified as a cause of a novel X-linked mental retardation (XLMR) syndrome.
100 μg
$199.00
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Ubiquigent™ Ube2B , Cat. No. 62-0004-020
Ube2B is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Koken et al. (1991). Ube2B shares 70% identity with its yeast homologue but lacks the acidic C-terminal domain. The ring finger proteins RAD5 and RAD18 interact with Ube2B and other members of the RAD6 pathway. In complex Ube2B and RAD18 trigger replication fork stalling at DNA damage sites during the post replicative repair process. Null mutations of the Ube2B gene in mice are associated with structural abnormalities in sperm and SNP analysis of human Ube2B variants has provided evidence for association of this gene with male infertility.
20 μg
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Ubiquigent™ Ube2B , Cat. No. 62-0004-100
Ube2B is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Koken et al. (1991). Ube2B shares 70% identity with its yeast homologue but lacks the acidic C-terminal domain. The ring finger proteins RAD5 and RAD18 interact with Ube2B and other members of the RAD6 pathway. In complex Ube2B and RAD18 trigger replication fork stalling at DNA damage sites during the post replicative repair process. Null mutations of the Ube2B gene in mice are associated with structural abnormalities in sperm and SNP analysis of human Ube2B variants has provided evidence for association of this gene with male infertility.
100 μg
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Ubiquigent™ Ube2C , Cat. No. 62-0007-020
Ube2C is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Townsley (Townsley et al., 1997). Ube2C shares 85% and 61% homology with frog and clam sequences respectively, and contains a 30 amino acid N-terminal extension. Ube2C binds APC11 and APC2 resulting in their autoubiquitylation and proteasomal degradation, a switch in the APC complex which causes sister chromatid separation and exit from mitosis. Ube2C has also been identified as a molecular marker useful in non small cell lung carcinoma (NSCLC) prognosis.
20 μg
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Ubiquigent™ Ube2C , Cat. No. 62-0007-100
Ube2C is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Townsley (Townsley et al., 1997). Ube2C shares 85% and 61% homology with frog and clam sequences respectively, and contains a 30 amino acid N-terminal extension. Ube2C binds APC11 and APC2 resulting in their autoubiquitylation and proteasomal degradation, a switch in the APC complex which causes sister chromatid separation and exit from mitosis. Ube2C has also been identified as a molecular marker useful in non small cell lung carcinoma (NSCLC) prognosis.
100 μg
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Ubiquigent™ Ube2D1 , Cat. No. 62-0010-020
Ube2D1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Scheffner et al. (1994). Ube2D1 shares 89% sequence identity with its Drosophila homologue and mediates E6/UBE3A (E6AP)-induced ubiquitylation of p53. Ubiquitylation of the yeast PTS1 import receptor (pex5p) has been demonstrated in an in vitro assay in the presence of the human Ube2D1 in combination with the ring domain of the yeast E3 ligase pex10p. Sequence encoding the stimulated Iron transport gene SFT overlaps with intron 7 and exon 6 of Ube2D1, and RT/PCR has shown significantly upregulated levels of Ube2D1 in livers of iron-overloaded patients with hereditary hemochromatosis.
20 μg
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Ubiquigent™ Ube2D1 , Cat. No. 62-0010-100
Ube2D1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Scheffner et al. (1994). Ube2D1 shares 89% sequence identity with its Drosophila homologue and mediates E6/UBE3A (E6AP)-induced ubiquitylation of p53. Ubiquitylation of the yeast PTS1 import receptor (pex5p) has been demonstrated in an in vitro assay in the presence of the human Ube2D1 in combination with the ring domain of the yeast E3 ligase pex10p. Sequence encoding the stimulated Iron transport gene SFT overlaps with intron 7 and exon 6 of Ube2D1, and RT/PCR has shown significantly upregulated levels of Ube2D1 in livers of iron-overloaded patients with hereditary hemochromatosis.
100 μg
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Ubiquigent™ Ube2D2 , Cat. No. 62-0012-020
Ube2D2 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Jensen et al. (1995). Ube2D2 shares 95% and 79% sequence identity with the Drosophila and S. cerevisiae homologues respectively. Ube2D2 can conjugate ubiquitin to targets in an E6AP dependent manner. Ube2D2 forms part of a ubiquitin E3 ligase complex with Cullin1, Skp1, Roc1 and BTRC. This complex has been shown to mediate activation of NFκB and promote degradation of phosphorylated IκBα. Co-immunoprecipitation has shown that the Shigella flexneri effector protein (OspG) interacts with Ube2D2. Glial cell missing homolog 1 (GCM1) is an important transcription factor regulating placental cell fusion and it has been shown that Ube2D2 is required for Skp1-Cullin-F-Box (SCF) E3 ligase mediated ubiquitylation of GCM1. Ube2D2 also supports mdm2 mediated ubiquitylation of p53.
20 μg
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Ubiquigent™ Ube2D2 , Cat. No. 62-0012-100
Ube2D2 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Jensen et al. (1995). Ube2D2 shares 95% and 79% sequence identity with the Drosophila and S. cerevisiae homologues respectively. Ube2D2 can conjugate ubiquitin to targets in an E6AP dependent manner. Ube2D2 forms part of a ubiquitin E3 ligase complex with Cullin1, Skp1, Roc1 and BTRC. This complex has been shown to mediate activation of NFκB and promote degradation of phosphorylated IκBα. Co-immunoprecipitation has shown that the Shigella flexneri effector protein (OspG) interacts with Ube2D2. Glial cell missing homolog 1 (GCM1) is an important transcription factor regulating placental cell fusion and it has been shown that Ube2D2 is required for Skp1-Cullin-F-Box (SCF) E3 ligase mediated ubiquitylation of GCM1. Ube2D2 also supports mdm2 mediated ubiquitylation of p53.
100 μg
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Ubiquigent™ Ube2D3 , Cat. No. 62-0014-020
Ube2D3 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the gene was first described by Jensen et al. (1995). The E3 ligase E6AP mediates the conjugation of ubiquitin to targets such as p53 via Ube2D3. Activation of the IKK complex is mediated by unanchored polyubiquitin chains formed by Ube2D3 and TRAF6. Zipper-Interacting Protein Kinase (ZIPK) is a serine/threonine kinase implicated in cell death and transcriptional regulation, Ube2D3 induces ZIPK accumulation in promyelocytic leukaemia protein nuclear bodies resulting in their ubiquitylation. Meibomian Cell Carcinoma (MCC) is a malignant tumour of the meibomian glands located in the eyelids. Ube2D3 has been identified by RT/PCR as one of five genes found to be upregulated in MCC tumours.
20 μg
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Ubiquigent™ Ube2D3 , Cat. No. 62-0014-100
Ube2D3 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the gene was first described by Jensen et al. (1995). The E3 ligase E6AP mediates the conjugation of ubiquitin to targets such as p53 via Ube2D3. Activation of the IKK complex is mediated by unanchored polyubiquitin chains formed by Ube2D3 and TRAF6. Zipper-Interacting Protein Kinase (ZIPK) is a serine/threonine kinase implicated in cell death and transcriptional regulation, Ube2D3 induces ZIPK accumulation in promyelocytic leukaemia protein nuclear bodies resulting in their ubiquitylation. Meibomian Cell Carcinoma (MCC) is a malignant tumour of the meibomian glands located in the eyelids. Ube2D3 has been identified by RT/PCR as one of five genes found to be upregulated in MCC tumours.
100 μg
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Ubiquigent™ Ube2D4 , Cat. No. 62-0017-020
Ube2D4 is a member of the E2 ubiquitin-conjugating enzyme family and the human gene was first described by Colland et al. (2004).
20 μg
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Ubiquigent™ Ube2D4 , Cat. No. 62-0017-100
Ube2D4 is a member of the E2 ubiquitin-conjugating enzyme family and the human gene was first described by Colland et al. (2004).
100 μg
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Ubiquigent™ Ube2E1 , Cat. No. 62-0019-020
Ube2E1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Nuber et al. (1996). Ube2E1 shares 74% sequence homology with Ube2D1 and has an N-terminal extension of approximately 40 amino acids. Ube2E1 modulates the transcriptional repression activity of Ataxin-1, the gene product of Spinocerebellar ataxia type 1 (SCA1). SCA1 is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration, which is caused by expansion of the polyglutamine tract in Ataxin-1. Ataxin-1 binds with Ube2E1 through its AXH domain and in vitro the rate of Ataxin-1 degradation is regulated by Ube2E1. Ube2E1 may have some therapeutic potential in the treatment of SCA1 by modulating the degradation of Ataxin-1.
20 μg
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Ubiquigent™ Ube2E1 , Cat. No. 62-0019-100
Ube2E1 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Nuber et al. (1996). Ube2E1 shares 74% sequence homology with Ube2D1 and has an N-terminal extension of approximately 40 amino acids. Ube2E1 modulates the transcriptional repression activity of Ataxin-1, the gene product of Spinocerebellar ataxia type 1 (SCA1). SCA1 is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration, which is caused by expansion of the polyglutamine tract in Ataxin-1. Ataxin-1 binds with Ube2E1 through its AXH domain and in vitro the rate of Ataxin-1 degradation is regulated by Ube2E1. Ube2E1 may have some therapeutic potential in the treatment of SCA1 by modulating the degradation of Ataxin-1.
100 μg
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Ubiquigent™ Ube2E2 , Cat. No. 62-0066-020
Ube2E2 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Kimura et al. (1997). The Ubc domain of Ube2E2 shares over 90% identity with human Ube2E1, mouse UbcM2, and Drosophila UbcD2. Ube2E2 has been shown to ubiquitylate the E3 ligase E6AP by binding to its HECT domain. A yeast two hybrid screen identified two Ube2E2 binding proteins, UbcH7-Associated Protein (H7-AP1) and Human Homologue of Drosophila ARIadne (HHARI); both of these proteins are characterized by the presence of a RING finger and In Between RING finger (IBR) domains. Ube2E2 has also been shown to bind the ubiquitin-protein ligase Parkin via its C-terminal ring-finger domain, resulting in ubiquitylation of the synaptic vesicle associated protein CDCrel-1.
20 μg
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Ubiquigent™ Ube2E2 , Cat. No. 62-0066-100
Ube2E2 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the human gene was first described by Kimura et al. (1997). The Ubc domain of Ube2E2 shares over 90% identity with human Ube2E1, mouse UbcM2, and Drosophila UbcD2. Ube2E2 has been shown to ubiquitylate the E3 ligase E6AP by binding to its HECT domain. A yeast two hybrid screen identified two Ube2E2 binding proteins, UbcH7-Associated Protein (H7-AP1) and Human Homologue of Drosophila ARIadne (HHARI); both of these proteins are characterized by the presence of a RING finger and In Between RING finger (IBR) domains. Ube2E2 has also been shown to bind the ubiquitin-protein ligase Parkin via its C-terminal ring-finger domain, resulting in ubiquitylation of the synaptic vesicle associated protein CDCrel-1.
100 μg
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Ubiquigent™ Ube2E3 , Cat. No. 62-0022-020
Ube2E3 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the gene was first described by Ito (Ito et al., 1999). Ube2E3 binds to the RING-finger proteins ARA54 and RNF8, thought to act as E3 ligases in the ubiquitylation of nuclear proteins. The epithelial Na+ channel (ENaC) is regulated by Ube2E3 and the E3 ligase NEDD4.2. Ube2E3 interacts with NEDD4.2 via its UBC domain and ubiquitylation of ENaC occurs by NEDD4.2 binding the PY motifs of its α, β and γ subunits. NEDD4.2 is a negative regulator of ENaC and deletions in the PY motifs of the β and γ subunits of ENaC cause Liddle's syndrome, an inherited form of hypertension. The loss of NEDD4.2 binding sites in mutated ENaC causes an increase in channel number at the cell surface and increased Na+ reabsorption by the distal nephron, resulting in hypertension.
20 μg
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Ubiquigent™ Ube2E3 , Cat. No. 62-0022-100
Ube2E3 is a member of the E2 ubiquitin-conjugating enzyme family and cloning of the gene was first described by Ito (Ito et al., 1999). Ube2E3 binds to the RING-finger proteins ARA54 and RNF8, thought to act as E3 ligases in the ubiquitylation of nuclear proteins. The epithelial Na+ channel (ENaC) is regulated by Ube2E3 and the E3 ligase NEDD4.2. Ube2E3 interacts with NEDD4.2 via its UBC domain and ubiquitylation of ENaC occurs by NEDD4.2 binding the PY motifs of its α, β and γ subunits. NEDD4.2 is a negative regulator of ENaC and deletions in the PY motifs of the β and γ subunits of ENaC cause Liddle's syndrome, an inherited form of hypertension. The loss of NEDD4.2 binding sites in mutated ENaC causes an increase in channel number at the cell surface and increased Na+ reabsorption by the distal nephron, resulting in hypertension.
100 μg
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Ubiquigent™ Ube2F , Cat. No. 62-0025-020
Ube2F is a member of the E2 conjugating enzyme family and the human gene was first described by Huang et al. (2009). Ube2F acts as a NEDD8 conjugating enzyme both in vitro and in vivo. Ube2F accepts the ubiquitin-like protein NEDD8 from the Uba3-NAE1 (APP-BP1/Uba3) E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction of Ube2F with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-Ube2F complex NEDDylates specific target proteins such as CUL5, a component of one of the many Cullin Ring Ligases (CRLs).
20 μg
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Ubiquigent™ Ube2F , Cat. No. 62-0025-100
Ube2F is a member of the E2 conjugating enzyme family and the human gene was first described by Huang et al. (2009). Ube2F acts as a NEDD8 conjugating enzyme both in vitro and in vivo. Ube2F accepts the ubiquitin-like protein NEDD8 from the Uba3-NAE1 (APP-BP1/Uba3) E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction of Ube2F with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-Ube2F complex NEDDylates specific target proteins such as CUL5, a component of one of the many Cullin Ring Ligases (CRLs).
100 μg
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Ubiquigent™ Ube2G1 , Cat. No. 62-0028-020
Ube2G1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Watanabe et al. (1996). Ube2G1 shares 74% sequence identity with UBC7 from C. elegans and a high degree of homology with UBC7 from other species. Expression of Ube2G1 and a helix-loop-helix transcription factor and member of the MYC/MAX superfamily (ROX/MNT) is decreased in medulloblastoma tumours. Haploinsufficiency of the human 17p13.3 region is associated with 35% to 50% of medulloblastomas, indicating the presence of one or more tumour suppressor genes which have not yet been identified.
20 μg
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Ubiquigent™ Ube2G1 , Cat. No. 62-0028-100
Ube2G1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Watanabe et al. (1996). Ube2G1 shares 74% sequence identity with UBC7 from C. elegans and a high degree of homology with UBC7 from other species. Expression of Ube2G1 and a helix-loop-helix transcription factor and member of the MYC/MAX superfamily (ROX/MNT) is decreased in medulloblastoma tumours. Haploinsufficiency of the human 17p13.3 region is associated with 35% to 50% of medulloblastomas, indicating the presence of one or more tumour suppressor genes which have not yet been identified.
100 μg
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Ubiquigent™ Ube2G2 , Cat. No. 62-0030-020
Ube2G2 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Katsanis and Fischer (1998). The Ube2G2 gene encodes a 165-amino-acid protein that shares 57% sequence identity with Ube2G1. Ube2G2 is involved in protein degradation, including a process known as Endoplasmic Reticulum-Associated Degradation (ERAD). Ube2G2 binds the E3 ligase GP78 and the affinity of this interaction is significantly increased by the G2BR domain on GP78. The Ube2G2/GP78 interaction results in the preassembly of Lys-48-linked ubiquitin chains on the catalytic cysteine of Ube2G2. A C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum - TEB4 – also catalyses Lys-48-linked polyubiquitylation employing Ube2G2 in vitro.
20 μg
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Ubiquigent™ Ube2G2 , Cat. No. 62-0030-100
Ube2G2 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Katsanis and Fischer (1998). The Ube2G2 gene encodes a 165-amino-acid protein that shares 57% sequence identity with Ube2G1. Ube2G2 is involved in protein degradation, including a process known as Endoplasmic Reticulum-Associated Degradation (ERAD). Ube2G2 binds the E3 ligase GP78 and the affinity of this interaction is significantly increased by the G2BR domain on GP78. The Ube2G2/GP78 interaction results in the preassembly of Lys-48-linked ubiquitin chains on the catalytic cysteine of Ube2G2. A C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum - TEB4 – also catalyses Lys-48-linked polyubiquitylation employing Ube2G2 in vitro.
100 μg
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Ubiquigent™ Ube2H , Cat. No. 62-0032-020
Ube2H is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Kaiser et al. (1994). Human Ube2H shares 54% identity with the yeast homologue (UbcH8) and full length forms of both the human and yeast enzymes showed similar enzymatic activities in vitro by catalyzing the ubiquitylation of histones. Ube2H has been mapped to a region on chromosome 7 and the gene has been identified as a candidate for involvement in an autistic disorder with neurodevelopmental complications. An association has also been made between Ube2H and the motor neuron disorder amyotrophic lateral sclerosis (ALS) where single strand conformation polymorphism (SSCP) analysis identified a known and sporadic polymorphism in the gene.
20 μg
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Ubiquigent™ Ube2H , Cat. No. 62-0032-100
Ube2H is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Kaiser et al. (1994). Human Ube2H shares 54% identity with the yeast homologue (UbcH8) and full length forms of both the human and yeast enzymes showed similar enzymatic activities in vitro by catalyzing the ubiquitylation of histones. Ube2H has been mapped to a region on chromosome 7 and the gene has been identified as a candidate for involvement in an autistic disorder with neurodevelopmental complications. An association has also been made between Ube2H and the motor neuron disorder amyotrophic lateral sclerosis (ALS) where single strand conformation polymorphism (SSCP) analysis identified a known and sporadic polymorphism in the gene.
100 μg
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Ubiquigent™ Ube2I , Cat. No. 62-0034-020
Ube2I is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Wang et al. (1996). The candidate tumour suppressor gene Fragile Histidine Triad (FHIT) located on 3p14.2 is deleted in many types of human cancer. Ube2I binds to FHIT and this interaction is thought to be involved in the degradation of S and M phase cyclins and cell cycle control. Proliferating Cell Nuclear Antigen (PCNA) a DNA polymerase sliding clamp involved in DNA synthesis and repair is a substrate for Ube2I. SUMOylation of Amyloid Precursor Protein (APP) is reported to be associated with decreased levels of beta amyloid (Abeta) aggregates, suggesting a role in the pathogenesis of Alzheimer’s Disease (AD). An investigation into single nucleotide polymorphisms (SNPs) in the Ube2I gene has shown an association between this and the risk of late onset AD.
20 μg
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Ubiquigent™ Ube2I , Cat. No. 62-0034-100
Ube2I is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Wang et al. (1996). The candidate tumour suppressor gene Fragile Histidine Triad (FHIT) located on 3p14.2 is deleted in many types of human cancer. Ube2I binds to FHIT and this interaction is thought to be involved in the degradation of S and M phase cyclins and cell cycle control. Proliferating Cell Nuclear Antigen (PCNA) a DNA polymerase sliding clamp involved in DNA synthesis and repair is a substrate for Ube2I. SUMOylation of Amyloid Precursor Protein (APP) is reported to be associated with decreased levels of beta amyloid (Abeta) aggregates, suggesting a role in the pathogenesis of Alzheimer’s Disease (AD). An investigation into single nucleotide polymorphisms (SNPs) in the Ube2I gene has shown an association between this and the risk of late onset AD.
100 μg
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Ubiquigent™ Ube2K , Cat. No. 62-0039-020
Ube2K is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Kalchman et al. (1996). Interaction and selective binding of Ube2K to the N-terminus of huntingtin, the causal gene product in Huntington’s disease has been demonstrated. Ube2K directs the synthesis of Lys63- or Lys48-linked ubiquitin chains on BRCA1. Ube2K was identified in a screen for novel SUMO targets, however attachment of SUMO to Ube2K in vitro severely impairs ubiquitin thioester and unanchored ubiquitin chain formation. The ubiquitin-proteasome system malfunction in Alzheimer’s disease (AD) has been attributed to neurotoxicity and proteasome inhibition by Abeta, which is mediated by an increase in the levels of Ube2K found in the brains of patients with AD.
20 μg
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Ubiquigent™ Ube2K , Cat. No. 62-0039-100
Ube2K is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Kalchman et al. (1996). Interaction and selective binding of Ube2K to the N-terminus of huntingtin, the causal gene product in Huntington’s disease has been demonstrated. Ube2K directs the synthesis of Lys63- or Lys48-linked ubiquitin chains on BRCA1. Ube2K was identified in a screen for novel SUMO targets, however attachment of SUMO to Ube2K in vitro severely impairs ubiquitin thioester and unanchored ubiquitin chain formation. The ubiquitin-proteasome system malfunction in Alzheimer’s disease (AD) has been attributed to neurotoxicity and proteasome inhibition by Abeta, which is mediated by an increase in the levels of Ube2K found in the brains of patients with AD.
100 μg
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Ubiquigent™ Ube2L3 , Cat. No. 62-0042-020
Ube2L3 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Moynihan et al. (1998). A protein complex comprising Ube2L3, the E3 ligase Parkin and alpha synuclein (alpha-Sp22) has been identified in which the substrate alpha-Sp22 becomes polyubiquitylated in normal human brains and targeted for degradation. Loss of Parkin function causes pathologic accumulation of alpha-Sp22 in the brain which is associated with Parkinson’s disease. Changes in levels of Ube2L3 during the cell cycle regulate entrance into and progression through S phase. Ube2L3 levels decrease during S-phase but are restored in G2, it is thought progression into G2 occurs by Ube2L3 modulation of the intra-S phase checkpoint mediated by Chk1.
20 μg
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Ubiquigent™ Ube2L3 , Cat. No. 62-0042-100
Ube2L3 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Moynihan et al. (1998). A protein complex comprising Ube2L3, the E3 ligase Parkin and alpha synuclein (alpha-Sp22) has been identified in which the substrate alpha-Sp22 becomes polyubiquitylated in normal human brains and targeted for degradation. Loss of Parkin function causes pathologic accumulation of alpha-Sp22 in the brain which is associated with Parkinson’s disease. Changes in levels of Ube2L3 during the cell cycle regulate entrance into and progression through S phase. Ube2L3 levels decrease during S-phase but are restored in G2, it is thought progression into G2 occurs by Ube2L3 modulation of the intra-S phase checkpoint mediated by Chk1.
100 μg
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Ubiquigent™ Ube2M , Cat. No. 62-0068-020
Ube2M is a member of the E2 conjugating enzyme family and the cDNA for Human Ube2M was first described by Osaka et al. (1998). A trapped ubiquitin like activation complex has been described for the NEDD8 pathway comprising, the E1 APP-BP1/Uba3, two NEDD8 molecules, Ube2M and MgATP. Thioester linkage of NEDD8 to APP-BP1-Uba3 results in an alternate E1 conformation that exposes two NEDD8 binding sites on the E2 enzyme. After transfer of the non-covalently bound NEDD8 to the E2, an alternate E1 conformation allows the release of the thioester bound NEDD8 product. Transference of the NEDD8 thioester linkage between E1 and E2 enzymes in this way can induce a conformational change and alter downstream signalling in the NEDD8 ubiquitin-like (Ubl) cascade. Following ionizing irradiation of a human esophageal cancer cell line a cDNA microarray screen found Ube2M to be upregulated suggesting a role for Ube2M in esophageal cancer.
20 μg
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Ubiquigent™ Ube2M , Cat. No. 62-0068-100
Ube2M is a member of the E2 conjugating enzyme family and the cDNA for Human Ube2M was first described by Osaka et al. (1998). A trapped ubiquitin like activation complex has been described for the NEDD8 pathway comprising, the E1 APP-BP1/Uba3, two NEDD8 molecules, Ube2M and MgATP. Thioester linkage of NEDD8 to APP-BP1-Uba3 results in an alternate E1 conformation that exposes two NEDD8 binding sites on the E2 enzyme. After transfer of the non-covalently bound NEDD8 to the E2, an alternate E1 conformation allows the release of the thioester bound NEDD8 product. Transference of the NEDD8 thioester linkage between E1 and E2 enzymes in this way can induce a conformational change and alter downstream signalling in the NEDD8 ubiquitin-like (Ubl) cascade. Following ionizing irradiation of a human esophageal cancer cell line a cDNA microarray screen found Ube2M to be upregulated suggesting a role for Ube2M in esophageal cancer.
100 μg
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Ubiquigent™ Ube2N , Cat. No. 62-0047-020
Ube2N is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Yamaguchi et al. (1996). In yeast, Ube2N forms a specific heteromeric complex with MMS2 a signaling component of the RAD6 pathway. Cytokine receptor signaling results in complex formation of protein kinases such as CD40 with TRAF2 and TRAF3, Ube2N, cellular inhibitor of apoptosis protein-1 (CIAP1) and -2 (CIAP2), IKK-α and MEKK1. Translocation of a TRAF2, Ube2N, and IKK-α complex from the membrane to the cytosol is initiated by a CIAP1/CIAP2-induced degradation of TRAF3 which results in activation of MEKK1 and MAP kinase cascades. Heterozygous Ube2N mice exhibit selectively impaired activation of signal transduction pathways initiated by TNFr and show reduced ubiquitylation of TRAF6. Reducing Ube2N activity may have therapeutic uses in controlling inflammatory responses.
20 μg
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Ubiquigent™ Ube2N , Cat. No. 62-0047-100
Ube2N is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Yamaguchi et al. (1996). In yeast, Ube2N forms a specific heteromeric complex with MMS2 a signaling component of the RAD6 pathway. Cytokine receptor signaling results in complex formation of protein kinases such as CD40 with TRAF2 and TRAF3, Ube2N, cellular inhibitor of apoptosis protein-1 (CIAP1) and -2 (CIAP2), IKK-α and MEKK1. Translocation of a TRAF2, Ube2N, and IKK-α complex from the membrane to the cytosol is initiated by a CIAP1/CIAP2-induced degradation of TRAF3 which results in activation of MEKK1 and MAP kinase cascades. Heterozygous Ube2N mice exhibit selectively impaired activation of signal transduction pathways initiated by TNFr and show reduced ubiquitylation of TRAF6. Reducing Ube2N activity may have therapeutic uses in controlling inflammatory responses.
100 μg
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Ubiquigent™ Ube2Q2 , Cat. No. 62-0069-020
Ube2Q2 is a member of the E2 conjugating enzyme family. The cloning of human Ube2Q2 was first described by Crawford and Piwnica-Worms. (2001). Ube2Q2 has been found to be up-regulated in 85% of head and neck squamous cell carcinoma tumours, with an increase of 2.4-fold compared to normal tissue. Ube2Q2 has been identified as a novel oncosuppressor that inhibits tumour growth and it is thought it could function as a novel diagnostic tool and potential therapeutic target for head and neck squamous cell carcinoma. Inhibition of Ube2Q2 following treatment of HeLa cells with Microtubule Inhibiting Agent (MIA) causes mitotic arrest and increased cytotoxicity, effects only observed in the absence of MIA suggesting Ube2Q2 is only involved in this response rather than having a more general role in mitosis.
20 μg
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Ubiquigent™ Ube2Q2 , Cat. No. 62-0069-100
Ube2Q2 is a member of the E2 conjugating enzyme family. The cloning of human Ube2Q2 was first described by Crawford and Piwnica-Worms. (2001). Ube2Q2 has been found to be up-regulated in 85% of head and neck squamous cell carcinoma tumours, with an increase of 2.4-fold compared to normal tissue. Ube2Q2 has been identified as a novel oncosuppressor that inhibits tumour growth and it is thought it could function as a novel diagnostic tool and potential therapeutic target for head and neck squamous cell carcinoma. Inhibition of Ube2Q2 following treatment of HeLa cells with Microtubule Inhibiting Agent (MIA) causes mitotic arrest and increased cytotoxicity, effects only observed in the absence of MIA suggesting Ube2Q2 is only involved in this response rather than having a more general role in mitosis.
100 μg
$199.00
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Ubiquigent™ Ube2R1 , Cat. No. 62-0054-020
Ube2R1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Plon et al. (1993). Casein Kinase type II (CK2) mediated phosphorylation of Ube2R1 increases ubiquitylation of Sic-1 in the presence of the E3 ligase S-phase kinase-associated protein 1/Cullin/F-box/Cdc4 (SCFCdc4) during cell cycle progression. Specific binding of CK2 phosphorylated Ube2R1 to beta-TRCP (β-TRCP) - the substrate recognition unit of the SCF ligase - enhances degradation of its substrate beta-catenin. Ube2R1 also catalyzes polyubiquitylation of a substrate recruited by the Skp1-Cullin 1-F-box protein-ROC1 E3 ubiquitin ligase. Downregulation of Ube2R1 following let-7 overexpression in primary fibroblasts results in reduced SCF activity, stabilization of the Wee1 kinase, and an increased fraction of the cells in G(2)/M.
20 μg
$99.00
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Ubiquigent™ Ube2R1 , Cat. No. 62-0054-100
Ube2R1 is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Plon et al. (1993). Casein Kinase type II (CK2) mediated phosphorylation of Ube2R1 increases ubiquitylation of Sic-1 in the presence of the E3 ligase S-phase kinase-associated protein 1/Cullin/F-box/Cdc4 (SCFCdc4) during cell cycle progression. Specific binding of CK2 phosphorylated Ube2R1 to beta-TRCP (β-TRCP) - the substrate recognition unit of the SCF ligase - enhances degradation of its substrate beta-catenin. Ube2R1 also catalyzes polyubiquitylation of a substrate recruited by the Skp1-Cullin 1-F-box protein-ROC1 E3 ubiquitin ligase. Downregulation of Ube2R1 following let-7 overexpression in primary fibroblasts results in reduced SCF activity, stabilization of the Wee1 kinase, and an increased fraction of the cells in G(2)/M.
100 μg
$199.00
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Ubiquigent™ Ube2S , Cat. No. 62-0056-020
Ube2S is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Liu et al. (1992). The tumour suppressor protein Von Hippel-Lindau (VHL) associates with and is targeted by Ube2S for ubiquitin-mediated proteolysis in human cell lines. Over expression of Ube2S increases tumour cell proliferation, invasion, and metastasis through the VHL-HIF pathway and has been found to correlate positively with HIF-1A in tumour cell line. Ube2S can elongate ubiquitin chains initiated by the E2 enzymes Ube2C and Ube2D1, enhancing the degradation of APC/C substrates by the proteasome. Recently Ube2S has been shown to assemble K11-specific chains for human and Drosophila APC/C. Chain specific activity of Ube2S is dependent on cell cycle-dependent association with the APC/C activators Cdc20 and Cdh1. Depletion of Ube2S has been shown to result in severe spindle defects and mitotic delay.
20 μg
$99.00
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Ubiquigent™ Ube2S , Cat. No. 62-0056-100
Ube2S is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Liu et al. (1992). The tumour suppressor protein Von Hippel-Lindau (VHL) associates with and is targeted by Ube2S for ubiquitin-mediated proteolysis in human cell lines. Over expression of Ube2S increases tumour cell proliferation, invasion, and metastasis through the VHL-HIF pathway and has been found to correlate positively with HIF-1A in tumour cell line. Ube2S can elongate ubiquitin chains initiated by the E2 enzymes Ube2C and Ube2D1, enhancing the degradation of APC/C substrates by the proteasome. Recently Ube2S has been shown to assemble K11-specific chains for human and Drosophila APC/C. Chain specific activity of Ube2S is dependent on cell cycle-dependent association with the APC/C activators Cdc20 and Cdh1. Depletion of Ube2S has been shown to result in severe spindle defects and mitotic delay.
100 μg
$199.00
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Ubiquigent™ Ube2T , Cat. No. 62-0070-020
Ube2T is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Zhang et al. (2000). Ube2T is integral to the Fanconi Anemia (FA) pathway for DNA damage repair. Ube2T binds to the C-terminal PH domain of FANCL the ubiquitin ligase subunit of the FA core complex, which leads to the monoubiquitylation of FANCD2 and FANCI. E3 ligase activity is not determined by assembly of the FA core complex but by the DNA damage-induced subcellular localization of the complex to chromatin. Ube2T and FANCD2 access this subcellular fraction independently and FANCD2 monoubiquitylation is regulated by the formation of an E2/E3 holoenzyme on chromatin. Ube2T expression has been analysed in lung cancer tissue and compared to normal human tissue. Ube2T was found to be significantly upregulated at both the protein and mRNA level suggesting involvement in the malignant cell phenotype.
20 μg
$99.00
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Ubiquigent™ Ube2T , Cat. No. 62-0070-100
Ube2T is a member of the E2 conjugating enzyme family and cloning of the human gene was first described by Zhang et al. (2000). Ube2T is integral to the Fanconi Anemia (FA) pathway for DNA damage repair. Ube2T binds to the C-terminal PH domain of FANCL the ubiquitin ligase subunit of the FA core complex, which leads to the monoubiquitylation of FANCD2 and FANCI. E3 ligase activity is not determined by assembly of the FA core complex but by the DNA damage-induced subcellular localization of the complex to chromatin. Ube2T and FANCD2 access this subcellular fraction independently and FANCD2 monoubiquitylation is regulated by the formation of an E2/E3 holoenzyme on chromatin. Ube2T expression has been analysed in lung cancer tissue and compared to normal human tissue. Ube2T was found to be significantly upregulated at both the protein and mRNA level suggesting involvement in the malignant cell phenotype.
100 μg
$199.00
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E3 Ligases
Ubiquigent™ CHIP , Cat. No. 63-0003-020
C-Terminus of Hsc70 Interacting Protein (CHIP) is a member of the E3 protein ligase family and cloning of the human gene was first described by Ballinger et al. (1999). The intrinsic E3 ligase activity of CHIP is conferred though a Ubox domain at the C-terminus of the protein. CHIP interacts with the Ube2D E2 enzyme family targeting the Heat Shock Cognate protein-70 (HSC70) for ubiquitylation. CHIP co-localises with alpha-synuclein in Lewy bodies and mediates alpha-synuclein degradation by both the proteasomal and lysosomal pathways. Cystic fibrosis arises from the misfolding and premature degradation of Cystic Fibrosis Transconductance Regulator (CFTR) carrying the deletion Phe508 (delF508). A cytosolic CHIP/Hsc70 complex cooperates with a ubiquitin ligase complex containing RMA1, Ube2J1, and derlin-1 to monitor the folding status of CFTR and delFl508 in the cytosol and target the mutant form (CFTR-DeltaF508) to the proteosome.
20 μg
$195.00
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Ubiquigent™ CHIP , Cat. No. 63-0003-100
C-Terminus of Hsc70 Interacting Protein (CHIP) is a member of the E3 protein ligase family and cloning of the human gene was first described by Ballinger et al. (1999). The intrinsic E3 ligase activity of CHIP is conferred though a Ubox domain at the C-terminus of the protein. CHIP interacts with the Ube2D E2 enzyme family targeting the Heat Shock Cognate protein-70 (HSC70) for ubiquitylation. CHIP co-localises with alpha-synuclein in Lewy bodies and mediates alpha-synuclein degradation by both the proteasomal and lysosomal pathways. Cystic fibrosis arises from the misfolding and premature degradation of Cystic Fibrosis Transconductance Regulator (CFTR) carrying the deletion Phe508 (delF508). A cytosolic CHIP/Hsc70 complex cooperates with a ubiquitin ligase complex containing RMA1, Ube2J1, and derlin-1 to monitor the folding status of CFTR and delFl508 in the cytosol and target the mutant form (CFTR-DeltaF508) to the proteosome.
100 μg
$395.00
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Deubiquitylating Enzymes
Ubiquigent­™ 6His-CYLD , Cat. No. 64-0010-050
CYLD is a cytoplasmic deubiquitylating enzyme belonging to the Ubiquitin Carboxy-terminal Hydrolase (UCH) family and cloning of the gene was first described by Bignell et al. (2000). CYLD comprises a Cytoskeletal-Associated Protein-Glycine-conserved (CAP-GLY) domain, a proline rich region, an SH3 binding domain and a sequence homology to the catalytic domain of a UCH. CYLD has been identified as a tumour suppressor protein and negatively regulates the c-Jun NH(2)-terminal kinase (JNK) signalling pathway by inhibiting the activation of Map-Kinase Kinase7 (MKK7). CYLD is a negative regulator of the NF-kappaB (NFκB) signalling pathway by inhibiting the TNFR-Associated Factor 2 (TRAF2) mediated activation of IKappaB Kinase (IKK). Mutated CYLD is known to be associated with cylindromatosis, multiple familial trichoepithelioma, and Brooke-Spiegler syndrome.
50 μg
$450.00
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Ubiquigent­™ 6His-UCHL1 , Cat. No. 64-0007-050
UCHL1 is a cysteine protease and member of the UCH family of ubiquitin C-terminal hydrolases. Cloning of the human UCHL1 gene was first described by Day and Thompson (1987). UCHL1 contains a catalytic triad consisting of a cysteine (Cys90), a histidine (His161), and an aspartate (Asp176) residue. UCHL1 is expressed predominantly in neurons, testis and ovary. In vivo UCHL1 has been shown to be involved in the regulation of the ubiquitin pool, apoptosis, learning and memory, and its absence in mice because of spontaneous intragenic deletions yields phenotypes with neurological defects. Mutations in UCHL1 have been implicated in Parkinson disease (PD); a point mutation near the active site that changes Ile93 to Met (I93M) has been linked to an increased risk of developing an autosomal-dominant form of PD.
50 μg
$195.00
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Ubiquigent­™ 6His-USP5 , Cat. No. 64-0002-050
Ubiquitin specific processing protease 5 (USP5) is a member of the cysteine protease enzyme family and cloning of the human gene was first described by Wilkinson et al.(1995). USP5 protein contains an N-terminal zinc finger ubiquitin-binding domain (ZNF-UBP), a ubiquitin-specific processing protease (UBP) domain containing the active-site cys and his boxes, and two ubiquitin-associated domains (UBA1 and UBA2). Crystal structures of the ZNF-UBP domain have revealed a deep binding pocket where the C-terminal diglycine motif of ubiquitin is inserted explaining the specificity of USP for an unmodified C-terminus on the proximal subunit of polyubiquitin. Recently USP5 has been identified in association with the 26S proteasome alongside other proteins known in complex as the UBL interactome.
50 μg
$195.00
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Ubiquigent­™ 6His-USP7 , Cat. No. 64-0003-050
Ubiquitin specific processing protease 7 (USP-7) is a member of the cysteine protease enzyme family and cloning of the gene in humans was first described by Everett et al. (1997). Overexpression of p53 and USP7 stabilizes p53 through the removal of ubiquitin moieties from polyubiquitylated p53. Inhibition of USP7 expression results in the accumulation and stabilisation of p53 protein. However, USP7 has been shown to stabilise mdm2 a ubiquitin ligase that promotes the degradation of p53. Thus USP7 appears to play multiple roles in regulating the p53/mdm2 pathway and maintaining steady-state levels of p53 in the cell. Due to the role USP7 has been shown to play in the regulation of p53 its importance as a therapeutic target for treating hematopoietic tumours has been highlighted.
50 μg
$395.00
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Ubiquigent™ GST-OTUB2 , Cat. No. 64-0012-050
OTUB2 is a cysteine protease and member of the Ovarian Tumor (OTU) protein super family. Cloning of the human OTUB2 gene was first described by Balakirev et al. (2003). OTUB2 contains Ubiquitin Interaction Motifs (UIMs) and Ubiquitin Associated (UBA) domains, as well as putative nuclear localization signals and a consensus LxxLL motif. De-ubiquitylation has emerged as a post translational mechanism for the activation of virus triggered type I interferon (IFN) (2) induction pathways. Integrative gene tissue array analysis has been used to locate disease relevant proteins to a linkage region associated with familial Amyotrophic Lateral Sclerosis (ALS)/frontotemporal dementia. Using this approach OTUB2 was identified as a disease relevant protein involved in TAU-1 and SOD1 induced motor neuron degeneration found in human sporadic ALS (SALS).
50 μg
$395.00
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E2scan™ Kit
Ubiquigent™ E2 Scan Kit , Cat. No. 67-0003-001
E2scan Kit is designed to facilitate the identification of E2 conjugating enzymes which support the ubiquitylation of substrate proteins catalysed by an E3 ligase and/or the auto-ubiquitylation of the E3 ligase itself. One kit contains all the reagents and buffers necessary to perform two ‘E2scans’ of the panel of 29 E2 conjugating enzymes. You need only provide your E3 ligase to be evaluated and substrate of interest (if required). A control E3 ligase (C-terminus of Hsc70 Interacting Protein; CHIP) and various control wells are also provided in order to carry out control auto-ubiquitylation assays or any other controls that you may wish to perform. A detailed user protocol is included.
1 Kit
$945.00
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