PLCgamma1 (N-terminal Region) (clone M156), anti-human, mouse, rat

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 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.

Immunogen: 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.

Specificity: The antibody detects a 150 kDa* protein in human A431, Hct116, and Jurkat cells, as well as in mouse brain.

Buffer/Storage:
Mouse monoclonal antibody purified with protein A chromatography is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.