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CSK Protein (His-GST)

Protéine Recombinant CSK exprimée dans Baculovirus infected Insect Cells.
N° du produit ABIN7320001
746,00 €
Plus frais de livraison 40,00 € et TVA
50 μg
Destination: France
Envoi sous 9 à 13 jours ouvrables

Aperçu rapide pour CSK Protein (His-GST) (ABIN7320001)

Antigène

Voir toutes CSK Protéines
CSK (C-Src tyrosine Kinase (CSK))

Type de proteíne

Recombinant

Activité biologique

Active

Origine

  • 14
  • 2
  • 1
  • 1
  • 1
Souris

Source

  • 6
  • 5
  • 3
  • 2
  • 1
  • 1
  • 1
Baculovirus infected Insect Cells

Pureté

> 85 % as determined by reducing SDS-PAGE.
  • Purification/Conjugué

    Cette CSK protéine est marqué à la His-GST.

    Fonction

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

    Séquence

    Met 1-Leu 450

    Attributs du produit

    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.

    Stérilité

    0.2 μm filtered

    niveau d'endotoxine

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

    Biological Activity Comment

    The specific activity was determined to be 70 nmol/min/mg using Poly(Glu, Tyr) 4:1 as substrate.
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  • Restrictions

    For Research Use only
  • Format

    Liquid

    Buffer

    Supplied as sterile solution of 20 mM Tris, 500 mM NaCl, pH 8.0, 10 % glycerol

    Stock

    -20 °C

    Stockage commentaire

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

    Date de péremption

    6 months
  • Antigène

    CSK (C-Src tyrosine Kinase (CSK))

    Autre désignation

    CSK/C-Src kinase

    Sujet

    AW212630,p50CSK,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 tail. 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.

    Poids moléculaire

    Calculated MW: 78.5 kDa

    Observed MW: 65 kDa

    Pathways

    TCR Signaling, EGFR Signaling Pathway, Cell-Cell Junction Organization, CXCR4-mediated Signaling Events
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