Enabling Protein Degradation Drug Discovery

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  • Name
    Catalogue Number
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  • Name:
    BRSK2 residues (2-674) [6His-tagged]
    Catalogue Number:
    50 µg
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  • Species
  • Source
    Sf21 insect cell-baculovirus expression
  • Quantity
    50 µg
  • Storage
  • Concentration
    1 mg/ml
  • Formulation
    50 mM Tris/HCl pH 7.5, 0.1 mM EGTA, 150 mM NaCl, 270 mM sucrose, 0.03% Brij, 0.1% b-Mercapto-ethanol, 1 mM Benzamidine, 0.2 mM PMSF
  • Molecular Weight
    ~78.3 kDa
  • Stability
    12 months at -70°C; aliquot as required
  • Protein Sequence
    Accession number: AAP97725.1. For full protein sequence information download the Certificate of Analysis pdf.
  • QA; Protein Identification
    Confirmed by mass spectrometry.
  • QA; Activity
    Activity Assay: The specific activity of His-BRSK2 was determined using the method described by Hastie et al. (2006) with the enzyme being assayed at several concentrations.  His-BRSK2 was incubated for 10 minutes at 30°C in kinase reaction buffer in the presence of CHKtide substrate (300µM) and [γ-32P]ATP (100µM). Duplicate reactions were stopped by spotting the assay mixture onto Whatman P81 paper - capturing the phosphorylated substrate.  The radioactivity incorporated was measured on a scintillation counter and the enzyme's mean specific activity was calculated. 

    His-BRSK2 specific activity: 333.7 Units/mg (333.7 Units/ml)

    1 Unit = 1 nmole of phosphate incorporated into the substrate in 1 minute


Protein ubiquitylation and protein phosphorylation are the two major mechanisms that regulate the functions of proteins in eukaryotic cells.  However, these different posttranslational modifications do not operate independently of one another, but are frequently interlinked to enable biological processes to be controlled in a more complex and sophisticated manner. Studying how protein phosphorylation events control the ubiquitin system and how ubiquitylation regulates protein phosphorylation has become a focal point of the study of cell regulation and human disease. Cloning of human Brain Specific Kinase 2 (BRSK2) was first described by Miura et al. (1998). BRSK2 is a member of the subfamily of protein kinases that include the AMP-activated protein kinase (AMPK) and, like AMPK itself, is activated by the tumour suppressor kinase LKB1 (Lizcano et al., 2004). As implied by its name BRSK2 is expressed in the brain where it plays an essential role in controlling neuronal cell polarisation. BRSK2 contains a ubiquitin-like domain adjacent to the kinase catalytic domain (Al-Hakim et al., 2008).


Al-Hakim AK, Zagorska A, Chapman L, Deak M, Peggie M, Alessi DR (2008) Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains. Biochem J 411, 249-60.

Hastie CJ, McLauchlan HJ, Cohen P (2006) Assay of protein kinases using radiolabeled ATP: a protocol. Nat Protoc 1, 968-71.

Miura K, Masuzaki H, Ishimaru T, Niikawa N, Jinno Y (1998) A HhaI/BstUI polymorphism in a novel gene at human chromosome 11p15.5. J Hum Genet 90, 283-4.

Lizcano JM, Goransson O, et al. (2004) LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1. EMBO J 23, 833-43.

Background kindly written by:

Sir Philip Cohen FRS, FRSE

University of Dundee

Director of the Medical Research Council Protein Phosphorylation Unit (1990-2012)


Director of the Scottish Institute for Cell Signalling incorporating the Protein Ubiquitylation Unit (2008-2012)


Co-Director of the Division of Signal Transduction Therapy (1998-2012)


Deputy Director of the Division of Signal Transduction Therapy (from July 2012)

Professor Cohen’s research group is studying the interplay between protein phosphorylation and protein ubiquitylation
in the regulation of innate immunity.