Product Name: SrcSubtide
Product Number: PE-01BJK95
Size: 200 µg      Price:12.00
1 mg      $US23.00
5 mg      64.00
Peptide Name: SrcSubtide

Product Use: For assaying the phosphotransferase activity of Src oncogene-encoded protein-tyrosine kinase (UniProt ID P12931).

Peptide Production Method: Solid-phase peptide synthesis

Peptide Sequence: KKGGEDDVYENVGG

Peptide Modifications N Terminus: Free amino

Peptide Modifications C Terminus: βAla-Cys

Peptide Molecular Mass Calculated: 1639.69 Da

Peptide Purity Percent after Synthesis and Purification: >50

Peptide Appearance: White powder

Peptide Form: Solid
Storage Conditions: -20°C

Peptide Recommended Enzyme: Src

Scientific Background: Src is a protein-tyrosine kinase of the TK group and Src family. It is a non-receptor protein-tyrosine kinase that is widely distributed from low to moderate levels in most human tissues with highest expression in pancreas and stomach. 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 activated by phosphorylation at S12, S75, Y419 and T420. S12 phosphorylation promotes interaction with PPP2R2C and Y410 phosphorylation induces interaction with Cbl-c. Phosphorylation at S17 may reduce phosphorylation at S12. Phosphorylation of S97 and Y530 inhibits Src phosphotransferase activity. 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. Src has also been linked with the development of colon cancer. Insertional mutagenesis studies in mice also support a role for this protein kinase in mouse cancer oncogenesis. Although mutations that increase the catalytic activity of Src are well known, such as loss of the inhibitory tyrosine phosphorylation site at the C-terminus of the kinase, it is not subject to higher rates of mutations in human tumours than most proteins.