Recombinant human Serine-arginine protein kinase 2, SRPK2, 10 µg

Background: Serine-arginine protein kinase 2 (SRPK2) as well as other SRPKs family members (SRPK1 and SRPK3), contains a PKC superfamily kinase domain separated by a unique spacer sequence in individual family members, indicating that specific SRPKs may be uniquely regulated by the spacer sequence. Each SRPK member has its unique expression pattern. Whereas SRPK1 is highly expressed in the testis; SRPK2 can be found mainly in the brain; and in contrast SRPK3 is a muscle-specific protein. SRPKs are constitutively active enzymes that require no post-translational modification to initiate the kinase activity. Nevertheless, their enzymatic activities can be regulated by the status of phosphorylation and subcellular localization e.g. Akt phosphorylates SRPK2, triggers its nuclear translocation and mediates cell cycle progression and cell death in neurons. SRPK2 phosphorylates serine/arginine domain-containing proteins and mediates pre-mRNA splicing and has an important role in controlling neuronal functions. SRPK2 may contribute to the formation of hyperphosphorylated tau and the pathogenesis of Alzheimer’s Disease.

Recombinant human protein kinase SRPK2 (Serine/arginine-rich protein-specific kinase 2), amino acids M1-S688 recombinant and active enzyme, N-terminally fused to GST-HIS6-Thrombin cleavage site, not activated by special procedures

Theoretical MW : 107.422 kDa (fusion proteins)
Expression system: Baculovirus infected Sf9 cells
Purification: One-step affinity purification using GSH-agarose
Storage buffer: 50 mM Tris-HCl, pH 8.0; 100 mM NaCl, 5 mM DTT, 4 mM reduced glutathione, 20% glycerol
Protein concentration: 0.330 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MSFC membrane
Specific activity : 52,000 pmol/mg min

Entrez Gene ID 6733 
UniProtKB P78362

Ordering information: shipped on dry ice

Product specific literature

Hong Y, Chan CB, Kwon IS, Li X, Song M, Lee HP, Liu X, Sompol P, Jin P, Lee HG, Yu SP, Ye K.(2012) “SRPK2 phosphorylates tau and mediates the cognitive defects in Alzheimer's disease.” J Neurosci. 28;32(48):17262-72.

Chan CB, Ye K.(2013) „Serine-arginine protein kinases: new players in neurodegenerative diseases?” Rev Neurosci.24(4):401-13.

Liang N, Zeng C, Tao KP1, Sou WH, Hsia HP, Qu D, Lau SN, Ngo JC. “Primary structural features of SR-like protein acinusS govern the phosphorylation mechanism by SRPK2.” Biochem J. 2014 Apr 1;459(1):181-91.