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Description
PE anti-PLCγ1 Phospho (Tyr783). Phospholipase C (PLC) enzymes cleave the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) into second messenger molecules inositol 1,4,5-triposphate (IP3) and diacylglycerol (DAG) in response to extracellular stimuli. IP3 causes the release of calcium from the endoplasmic reticulum to begin an intracellular signaling cascade, while DAG activates Protein Kinase C. There are four families of PLCs. PLC gamma (PLCγ) uniquely contains SRC domains SH2 and SH3. Receptor tyrosine kinases interact with these SRC domains to enzymatically activate PLCγ1 via phosphorylation at Tyr 783. PLCγ1 is essential for cell proliferation, differentiation, and motility. Overexpression or activation of PLCγ1 has been implicated in breast and prostate cancers, as well as cancer cell invasion.
Immunogen
Synthetic peptide from human plcy1 phosphorylated at Try783 emulsified in CFA