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Mouse CSK / C-Src kinase Protein

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Mouse CSK Protein Product Information
Protein Construction:A DNA sequence encoding the mouse CSK (P41241 ) (Met 1-Leu 450) was expressed and purified with two additional amino acids (Gly & Pro ) at the N-terminus.
Expressed Host:Baculovirus-Insect Cells
Shipping:Kinases are highly recommended to be shipped at frozen temperature with blue ice or dry ice.
Shipment made at ambient temperature may seriously affect the activity of the ordered products.
Mouse CSK Protein QC Testing
Purity:> 90 % as determined by SDS-PAGE
Bio-Activity:Kinase activity untested
Endotoxin:< 1.0 EU per μg of the protein as determined by the LAL method
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Gly
Molecule Mass:The recombinant mouse CSK consists of 452 amino acids and predicts a molecular mass of 50.9 KDa. It migrates as an approximately 46 KDa band in SDS-PAGE under reducing conditions.
Formulation:Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 8.0.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Mouse CSK Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Mouse CSK Protein SDS-PAGE
Mouse CSK / C-Src kinase Protein SDS-PAGE
Other CSK Recombinant Protein Products
C-Src Kinase / CSK Background

The tyrosine kinase c-Src has been implicated as a modulator of cell proliferation, spreading, and migration. These functions are also regulated by Met. The structure of a large fragment of the c-Src kinase comprises the regulatory and kinase domains and the carboxy-terminal tall. c-Src kinase interactions among domains and is stabilized by binding of the phosphorylated tail to the SH2 domain. This molecule is locked in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. The protein-tyrosine kinase activity of c-Src kinase is inhibited by phosphorylation of tyr527, within the c-Src c-terminal tail. Genetic and biochemical data have suggested that this negative regulation requires an intact Src homology 2 (SH2) domain. Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity. Experiments have suggested that c-Src kinase plays a role in the biological behaviour of colonic carcinoma cells induced by migratory factors such as EGF, perhaps acting in conjunction with FAK to regulate focal adhesion turnover and tumour cell motility. Furthermore, although c-Src kinase has been implicated in colonic tumour progression, in the adenoma to carcinoma in vitro model c-Src is not the driving force for this progression but co-operates with other molecules in carcinoma development.


Mouse C-Src Kinase / CSK References
  • Brauninger A. et al.,1992, Gene. 110: 205-11.
  • Sondhi D. et al., 1999, Biochemistry. 38 (34): 11147-55.
  • Ogawa A. et al., 2002, J Biol Chem. 277 (17): 14351-4.
  • Cole PA. et al., 2003, Curr Opin Chem Biol. 7 (5): 580-5.
  • Baumeister U. et al., 2005,EMBO J. 24 (9): 1686-95.
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    Catalog: 50893-MNCB-20
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