c-Src (phospho-Tyr-215) Blocking Peptide
€155.00
In stock
SKU
ECM-SX1375
Background:
c-Src was the first proto-oncogenic non-receptor tyrosine kinase characterized in human. The Src family is composed of nine members in vertebrates, including c-Src, Yes, Fgr, Yrk, Fyn, Lyn, Hck, Lck, and Blk. Src-family kinases transduce signals that are involved in the control of a variety of cellular processes, including proliferation, differentiation, motility, and adhesion. Src-family kinases contain an N-terminal cell membrane anchor followed by SH3 and SH2 domains. The activity of c-Src is regulated by tyrosine phosphorylation at multiple sites. Tyrosine 418 is autophosphorylated following c-Src activation. Tyrosine 215 in the SH2 domain of c-Src is phosphorylated following growth factor receptor activation. Both Tyr-215 and Tyr-418 phosphorylation increases tyrosine kinase activity, while phosphorylation of Tyr-530 downregulates c-Src kinase activity. Thus, tyrosine phosphorylation of c-Src is critical for regulating its kinase activity.
Sequence: Phospho-c-Src (Tyr-215) synthetic peptide corresponds to amino acid residues around tyrosine 215 of human c-Src. This peptide sequence has homology to other Src kinase family members, such as hck, fyn, csk, and yes.
Specificity: The peptide is specifically recognized by anti-c-Src (Tyr-215) phospho-specific antibody (SP1371) in ELISA, and has been shown to block the reactivity of SP1371 during Western blot. In addition, the peptide is recommended for use in blocking SP1371 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
c-Src was the first proto-oncogenic non-receptor tyrosine kinase characterized in human. The Src family is composed of nine members in vertebrates, including c-Src, Yes, Fgr, Yrk, Fyn, Lyn, Hck, Lck, and Blk. Src-family kinases transduce signals that are involved in the control of a variety of cellular processes, including proliferation, differentiation, motility, and adhesion. Src-family kinases contain an N-terminal cell membrane anchor followed by SH3 and SH2 domains. The activity of c-Src is regulated by tyrosine phosphorylation at multiple sites. Tyrosine 418 is autophosphorylated following c-Src activation. Tyrosine 215 in the SH2 domain of c-Src is phosphorylated following growth factor receptor activation. Both Tyr-215 and Tyr-418 phosphorylation increases tyrosine kinase activity, while phosphorylation of Tyr-530 downregulates c-Src kinase activity. Thus, tyrosine phosphorylation of c-Src is critical for regulating its kinase activity.
Sequence: Phospho-c-Src (Tyr-215) synthetic peptide corresponds to amino acid residues around tyrosine 215 of human c-Src. This peptide sequence has homology to other Src kinase family members, such as hck, fyn, csk, and yes.
Specificity: The peptide is specifically recognized by anti-c-Src (Tyr-215) phospho-specific antibody (SP1371) in ELISA, and has been shown to block the reactivity of SP1371 during Western blot. In addition, the peptide is recommended for use in blocking SP1371 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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