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CSK Protein (GST tag)

CSK Origin: Human Host: Baculovirus infected Insect Cells Recombinant > 92 % as determined by reducing SDS-PAGE. Active
Catalog No. ABIN7317088
  • Target See all CSK Proteins
    CSK (C-Src tyrosine Kinase (CSK))
    Protein Type
    Recombinant
    Biological Activity
    Active
    Origin
    • 9
    • 3
    • 1
    • 1
    • 1
    Human
    Source
    • 3
    • 3
    • 2
    • 2
    • 2
    • 2
    • 1
    Baculovirus infected Insect Cells
    Purification tag / Conjugate
    This CSK protein is labelled with GST tag.
    Purpose
    Recombinant Human CSK/C-Src kinase Protein (GST Tag)(Active)
    Sequence
    Met 1-Leu 450
    Characteristics
    A DNA sequence encoding the human CSK (NP_004374.1) (Met 1-Leu 450) was fused with the GST tag at the N-terminus.
    Purity
    > 92 % as determined by reducing SDS-PAGE.
    Endotoxin Level
    < 1.0 EU per μg as determined by the LAL method.
    Biological Activity Comment
    The specific activity was determined to be 127 nmol/min/mg using Poly(Glu,Tyr) 4:1 as substrate.
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  • Restrictions
    For Research Use only
  • Format
    Frozen, Liquid
    Buffer
    Supplied as sterile 20 mM Tris, 500 mM NaCl, 0.5 mM PMSF, pH 7.4
    Storage
    -20 °C
    Storage Comment
    Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
  • 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: MGC117393,CSK

    Molecular Weight
    77 kDa
    NCBI Accession
    NP_004374
    Pathways
    TCR Signaling, EGFR Signaling Pathway, Cell-Cell Junction Organization, CXCR4-mediated Signaling Events
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