Recombinant Mouse CSK/C-Src kinase Protein (His & GST Tag)(Active) | PKSM040291

Recombinant Mouse CSK/C-Src kinase Protein (His & GST Tag)(Active) | PKSM040291 | Gentaur US, UK & Europe Disrtribition

Synonyms: AW212630;p50CSK

Active Protein: Active protein

Activity: A DNA sequence encoding the mouse CSK (P41241?) (Met 1-Leu 450) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Protein Construction: A DNA sequence encoding the mouse CSK (P41241?) (Met 1-Leu 450) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Fusion Tag: N-His-GST

Species: Mouse

Expressed Host: Baculovirus-Insect Cells

Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.

Purity: > 85 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.

Molecular Mass: 78.5 kDa

Formulation: Supplied as sterile 20mM Tris, 500mM NaCl, pH 8.0, 10% glycerol

Reconstitution: Not Applicable

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. References

Research Area: N/A