c-src

pp60 c-src (521-533) (phosphorylated) acetate is a regulator of focal adhesion formation and cell spreading. pp60 c-src (521-533) (phosphorylated) acetate also regulates cell motility and is a key component in the signaling pathway triggered by the motogenic hyaluronan receptor RHAMM.

Peptide corresponding to the pp60c-src carboxy terminal regulatory domain; phosphorylated at Tyr527. Binds to pp60c-src and pp60v-src at the SH2 domain, suppressing their tyrosine kinase activity and transforming potential.

P60c-src substrate II is a potent pentapeptide substrate for the tyrosine kinase pp60c-src [1].

Phosphorylated p60c-src substrate II is a pentapeptide and a phosphorylated polypeptide form of p60c-src substrate II. Phosphorylation is a critical post-translational modification (post-translationmodification) vital for biological regulatory processes [1].

Tyr-Ile-Tyr-Gly-Ser-Phe-Lys is a polypeptide molecule with the sequence YIYGSFK.

Tyrosine Kinase Peptide 1 is a control substrate peptide used in c-Src assay.

ApolipoproteinKV domain (67-77) is an 11-amino-acid peptide isolated from the KV domain of human apolipoprotein a (ApoA), known for its anti-angiogenic and anti-tumor activities. It targets the angiogenesis c-Src/ERK pathway by blocking activation signals received from vascular endothelial growth factor (VEGF). ApolipoproteinKV domain (67-77) is applicable in cancer research.