PKCalpha (phospho-Ser-657/Tyr-658) Blocking Peptide
€155.00
In stock
SKU
ECM-PX1095
Background:
The Protein Kinase C (PKC) family of homologous serine/threonine protein kinases is involved in a number of processes such as growth, differentiation, and cytokine secretion. At least eleven isozymes have been described. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half interacts with PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester, while the C-terminal half contains the catalytic domain. The conventional PKC subfamily (α, β1, βII, and γ) is regulated by both Ca2+ and diacylglycerol. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters and growth factors. The phosphorylation of multiple sites in conventional PKCs regulates their activity. In mast cells, FceRI stimulation leads to phosphorylation of tyrosine 658 and 662 of PKCα and PKCβI respectively. This phosphorylation requires autophosphorylation of serine 657 and 661 in these respective kinases.
Sequence: Phospho-PKCα (Ser-657/Tyr-658) synthetic peptide corresponds to amino acid residues around serine 657 and tyrosine 658 of human PKCα. This sequence is similar to the conserved sites in rat and mouse, and has high homology to dual sites in human, rat, and mouse PKCβI (Ser-661/Tyr-662) and PKCγ (Thr-674/Tyr-675).
Specificity: The peptide is specifically recognized by anti-PKCα (Ser-657/Tyr-658) phospho-specific antibody (PP1091) in ELISA, and has been shown to block the reactivity of PP1091 during Western blot. In addition, the peptide is recommended for use in blocking PP1091 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.
The Protein Kinase C (PKC) family of homologous serine/threonine protein kinases is involved in a number of processes such as growth, differentiation, and cytokine secretion. At least eleven isozymes have been described. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half interacts with PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester, while the C-terminal half contains the catalytic domain. The conventional PKC subfamily (α, β1, βII, and γ) is regulated by both Ca2+ and diacylglycerol. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters and growth factors. The phosphorylation of multiple sites in conventional PKCs regulates their activity. In mast cells, FceRI stimulation leads to phosphorylation of tyrosine 658 and 662 of PKCα and PKCβI respectively. This phosphorylation requires autophosphorylation of serine 657 and 661 in these respective kinases.
Sequence: Phospho-PKCα (Ser-657/Tyr-658) synthetic peptide corresponds to amino acid residues around serine 657 and tyrosine 658 of human PKCα. This sequence is similar to the conserved sites in rat and mouse, and has high homology to dual sites in human, rat, and mouse PKCβI (Ser-661/Tyr-662) and PKCγ (Thr-674/Tyr-675).
Specificity: The peptide is specifically recognized by anti-PKCα (Ser-657/Tyr-658) phospho-specific antibody (PP1091) in ELISA, and has been shown to block the reactivity of PP1091 during Western blot. In addition, the peptide is recommended for use in blocking PP1091 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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