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C-Src Kinase / CSK  Protein, Antibody, ELISA Kit, cDNA Clone

Description: Active  
Expression host: Baculovirus-Insect Cells  
10740-H09B-50
10740-H09B-20
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20 µg 
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Description: Active  
Expression host: Baculovirus-Insect Cells  
50893-M20B-50
50893-M20B-20
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20 µg 
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Expression host: Baculovirus-Insect Cells  
50893-MNCB-50
50893-MNCB-20
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20 µg 
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    C-Src Kinase / CSK Summary & Protein Information

    C-Src Kinase / CSK Background

    Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-ProRule:PRU10028}.
    Subunit structure: Homodimer (via SH3-domain) (PubMed:19888460). Interacts with PTPN22 (PubMed:15208781). Interacts with phosphorylated SIT1, PAG1, LIME1 and TGFB1I1; these interactions serve to recruit CSK to the membrane where it can phosphorylate and inhibit Src-family kinases (PubMed:11433379, PubMed:10790433, PubMed:14610046, PubMed:10838081). Interacts with SRCIN1 (PubMed:17525734). Interacts with RHOH (PubMed:20851766). Interacts (via SH2 domain) with SCIMP (PubMed:21930792). {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:10838081, ECO:0000269|PubMed:11433379, ECO:0000269|PubMed:14610046, ECO:0000269|PubMed:15208781, ECO:0000269|PubMed:17525734, ECO:0000269|PubMed:20851766, ECO:0000269|PubMed:21930792}.
    Domain: The architecture of this protein is similar to that of Src-family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain, and a C-terminal kinase domain.
    Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Mainly cytoplasmic, also present in lipid rafts. {ECO:0000250}.
    Tissue specificity: Expressed in lung and macrophages. {ECO:0000269|PubMed:1371489}.
    Post-translational: Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated. {ECO:0000269|PubMed:11181701, ECO:0000269|PubMed:9148770}.
    Sequence similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 SH2 domain. {ECO:0000255|PROSITE-ProRule:PRU00191}.; Contains 1 SH3 domain. {ECO:0000255|PROSITE-ProRule:PRU00192}.
    General information above from UniProt

    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

    C-Src Kinase / CSK Alternative Name

    CSK,c-Src Kinase,c-Src tyrosine kinase,MGC117393,SRC, [human]
    p50CSK, [Mouse]
    p50CSK,AW212630, [mus-musculus]

    C-Src Kinase / CSK Related Studies

  • 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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