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

製品の説明: Active  
発現宿主: Baculovirus-Insect Cells  
  • Slide 1
10740-H09B-20
10740-H09B-50
20 µg 
50 µg 
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製品の説明: Active  
発現宿主: Baculovirus-Insect Cells  
  • Slide 1
50893-M20B-20
50893-M20B-50
20 µg 
50 µg 
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発現宿主: Baculovirus-Insect Cells  
  • Slide 1
50893-MNCB-20
50893-MNCB-50
20 µg 
50 µg 
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C-Src Kinase / CSK 関連経路

C-Src Kinase / CSK サマリー & タンパク質情報

C-Src Kinase / CSK 背景

遺伝子の概要: This gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this gene.
General information above from NCBI
触媒活性: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
サブユニット構造: Homodimer (via SH3-domain). Interacts with PTPN8 (By similarity). 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. Interacts with SRCIN1. Interacts with RHOH. Interacts (via SH2 domain) with SCIMP.
ドメイン: 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.
細胞内位置: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Mainly cytoplasmic, also present in lipid rafts (By similarity).
組織特異性: Expressed in lung and macrophages.
翻訳後: Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated.
シーケンスの類似性: Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily.
Contains 1 protein kinase domain.
Contains 1 SH2 domain.
Contains 1 SH3 domain.
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 代替名

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

C-Src Kinase / CSK 関連研究

  • 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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