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Src1, Active

A proto-oncogene
Catalog #: 7750
SKU-Size Size Price Qty
7750-5 5 μg
$295.00
7750-100 100 μg
$3,950.00
More Sizes Get Quote

Product Details

Alternate Name Src, v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog, Class E basic helix-loop-helix protein 74, Short name=bHLHe74, Protein Hin-2, RIP160, Renal carcinoma antigen NY-REN-52, Steroid receptor coactivator 1
Gene Symbol SRC
Gene ID 6714
Accession # P12931
Source E.coli
Appearance Liquid
Physical Form Description Recombinant proteins in storage buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.25 mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, 25% glycerol).
Molecular Weight 85.0 kDa
Purity by SDS-PAGE ≥90%
Handling Centrifuge the vial prior to opening.
Storage Conditions -80°C
Shipping Conditions Dry Ice
USAGE For Research Use Only! Not to be used in humans

Details

Src family belongs to non-receptor tyrosine kinases. Src was originally identified as a transforming protein of the Rous sarcoma virus (RSV) that had enzymatic ability to phosphorylate tyrosine in protein substrates. Src is overexpressed and activated in a large number of human malignancies and has been linked to the development of cancer and progression to distant metastases. In addition to increasing cell proliferation, a key role of Src in cancer seems to be the ability to promote invasion and motility, functions that might contribute to tumour progression. Oncogenic forms of the Src alter cell structure, in particular the actin cytoskeleton and the adhesion networks that control cell migration, and also transmit signals that regulate proliferation and cell survival. Recent work indicates that Src plays a role in these functions by influencing the RhoA-ROCK pathway that controls contractile actin filament assembly, the STAT family of transcription factors needed for transformation, and the Cbl ubiquitin ligase that controls Src protein levels. These studies also shed light on the role of focal adhesion kinase (FAK) downstream of v-Src and other signaling pathways in controlling migration, invasion and survival of transformed cells. Src directly phosphorylates integrins and can also modulate R-Ras activity. Moreover, it stimulates the E-cadherin regulator Hakai, interacts with and phosphorylates the novel podosome-linked adaptor protein Fish, and progressively phosphorylates the gap junction component connexion 43. In addition to the above functions and substrates, the role in cellular physiology of Src is continually expanding.


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