PLCgamma1 (phospho-Tyr-775) Blocking Peptide
€155.00
In stock
SKU
ECM-PX1495
Background:
Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors, and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ, and PLCε. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCδ is activated by both receptor and nonreceptor tyrosine kinases. PLCγ1 forms a complex with EGF and PDGF receptors, which leads to phosphorylation at tyrosine 771, 783, and 1245. In addition, antigen receptor-induced activation of PLCγ1 leads to phosphorylation at both Tyr-775 and Tyr-783. These two sites are equally important for activation of enzymatic activity.
Sequence: PLCγ1 (Tyr-775) synthetic peptide corresponds to amino acids around tyrosine 775 in human PLCγ1. This sequence has high homology to the conserved site in rat and mouse PLCγ1, and has low homology to PLCγ2.
Specificity: The peptide is specifically recognized by anti-PLCγ1 (Tyr-775) phospho-specific antibody (PP1491) in ELISA, and has been shown to block the reactivity of PP1491 during Western blot. In addition, the peptide is recommended for use in blocking PP1491 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.
Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors, and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ, and PLCε. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCδ is activated by both receptor and nonreceptor tyrosine kinases. PLCγ1 forms a complex with EGF and PDGF receptors, which leads to phosphorylation at tyrosine 771, 783, and 1245. In addition, antigen receptor-induced activation of PLCγ1 leads to phosphorylation at both Tyr-775 and Tyr-783. These two sites are equally important for activation of enzymatic activity.
Sequence: PLCγ1 (Tyr-775) synthetic peptide corresponds to amino acids around tyrosine 775 in human PLCγ1. This sequence has high homology to the conserved site in rat and mouse PLCγ1, and has low homology to PLCγ2.
Specificity: The peptide is specifically recognized by anti-PLCγ1 (Tyr-775) phospho-specific antibody (PP1491) in ELISA, and has been shown to block the reactivity of PP1491 during Western blot. In addition, the peptide is recommended for use in blocking PP1491 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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