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Background: Serine-arginine protein kinase 1 (SRPK1) as well as other SRPKs family members, 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. Deletion of the spacer region alters SRPK1 cellular residence from primarily localized in cytoplasm to almost exclusively in nuclei. SRPK1 is overexpressed in multiple cancer types, including breast, colon, ovarian, glioma and pancreatic carcinoma and its expression has been strongly associated with progression, poor survival, tumorigenesis, proliferation, metastasis and apoptosis. SRPK1 mainly phosphorylates specific amino acids of proteins rich in serine/arginine repeats known as SR-domain proteins that participate in precursor mRNA translation, processing and splicing, chromatin reconstruction, cell cycle progression, and remodeling of cellular structures. Additionally, SRPKs support phosphorylation-dependent transport of SR proteins from the cytoplasm to the nucleus via an SR-specific transportin protein, TRN-SR2.
Recombinant Human SRPK1 (Serine/arginine-rich protein-specific kinase 1), active enzyme, N-terminally fused to GST-HIS6-Thrombin cleavage site, kinase was not activated by special procedures
Theoretical MW : 104.220 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: 0.250 mg/ml (Bradford method using BSA as standard protein)
Method for determination of Km value & specific activity: Filter binding assay MSPH membrane
Specific activity : 91,000 pmol/mg min
Entrez Gene ID: 6732
UniProtKB: Q96SB4
Ordering information: shipped on dry ice
Aubol BE, Wu G, Keshwani MM, Movassat M, Fattet L, Hertel KJ, Fu XD, Adams JA. (2016) “Release of SR Proteins from CLK1 by SRPK1: A Symbiotic Kinase System for Phosphorylation Control of Pre-mRNA Splicing.” Mol Cell. ;63(2):218-28
Zhou B, Li Y, Deng Q, Wang H, Wang Y, Cai B, Han ZG.(2013) “SRPK1 contributes to malignancy of hepatocellular carcinoma through a possible mechanism involving PI3K/Akt.” Mol Cell Biochem. 2013 Jul;379(1-2):191-9.
Ding JH, Zhong XY, Hagopian JC, Cruz MM, Ghosh G, Feramisco J, Adams JA, Fu XD.(2006) “Regulated cellular partitioning of SR protein-specific kinases in mammalian cells.” Mol Biol Cell. 2006 Feb;17(2):876-85.
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