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CSK Protein

CSK Origin: Mouse Host: Baculovirus infected Insect Cells Recombinant > 90 % as determined by SDS-PAGE
Catalog No. ABIN7320121
  • Target See all CSK Proteins
    CSK (C-Src tyrosine Kinase (CSK))
    Protein Type
    Recombinant
    Origin
    • 9
    • 1
    • 1
    • 1
    • 1
    Mouse
    Source
    • 3
    • 3
    • 2
    • 2
    • 2
    • 1
    Baculovirus infected Insect Cells
    Purpose
    Recombinant Mouse CSK/C-Src kinase Protein (Active)
    Sequence
    Met 1-Leu 450
    Characteristics
    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.
    Purity
    > 90 % as determined by SDS-PAGE
    Endotoxin Level
    < 1.0 EU per μg of the protein as determined by the LAL method.
    Biological Activity Comment
    Kinase activity untested
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    Discover our top product CSK Protein
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Reconstitution
    Please refer to the printed manual for detailed information.
    Buffer
    Lyophilized from sterile 20 mM Tris, 500 mM NaCl, 10 % glycerol, pH 8.0
    Storage
    4 °C,-20 °C,-80 °C
    Storage Comment
    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
  • Target
    CSK (C-Src tyrosine Kinase (CSK))
    Alternative Name
    CSK/C-Src kinase (CSK Products)
    Synonyms
    AW212630 Protein, C-terminal Src kinase Protein, c-src tyrosine kinase Protein, CSK, non-receptor tyrosine kinase Protein, CSK Protein, Csk Protein
    Background

    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

    Synonym: AW212630,p50CSK

    Molecular Weight
    50.9 kDa
    UniProt
    P41241
    Pathways
    TCR Signaling, EGFR Signaling Pathway, Cell-Cell Junction Organization, CXCR4-mediated Signaling Events
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