Anti-PLCγ1 (N-terminal region) Antibody

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 regulates 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.

Our PLCγ1 (N-terminal region) primary antibody from PhosphoSolutions is mouse monoclonal. It detects chicken, human, mouse, and rat PLCγ1 (N-terminal region) and is Protein A purified. It is great for use in WB, ICC, IP.

Clone (M156) was generated from a synthetic peptide corresponding to amino acids in the N-terminal region of human PLCγ1. This sequence is highly conserved in rat and mouse PLCγ1, and has low homology to PLCγ2.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.