The Phospholipase C (PLC) isozymes hydrolyze phosphatidyl inositol phosphate to inositol triphosphate and diacylglycerol. The former
causes release of calcium from the endoplasmic reticulum, while the latter is an activator of Protein Kinase C. Within the PLC family, PLCγ is
the only member that contains SH2 and SH3 domains. These domains enable it to interact with receptor tyrosine kinases and become
enzymatically activated via phosphorylation. It exists as two isoforms: 1) PLCγ1, which is ubiquitously expressed, and 2) PLCγ2, found
primarily in the lymphoid system. PLCγ is essential for growth factor-induced cell motility and mitogenesis. PLCγ1-null mice exhibit retarded
embryonic growth and lethality in midgestation. In addition, PDGF stimulation leads to phosphorylation of PLCγ at Tyr 783, and activation of
hydrolyzing activity. Overexpression of PLCγ is evident in several forms of cancer and it has been identified as a key mediator of
PDGF-dependent cellular transformation. Thus, regulation of PLCγ activity by growth factors is involved in cell growth and transformation.
原厂资料：
注意事项：
1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
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