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-biphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5- triphosphate (IP3) and diacylglycerol (DAG). At least four families of PLC5, PLCbeta, PLCgamma, PLCdelta and PLCepsilon have been identified so far. The PLCbeta subfamily includes four members, PLCbeta1-4. All four members of the subfamily are activated by alpha-or beta-gamma-subunits of the heterotrimeric G-proteins (2,3). Phosphorylation is one of the key mechanisms that regulates the activity of PLC. Phosphorylation of serine 1105 by PKA or PKC inhibits PLCbeta3 activity (4,5). Serine 537 of PLCbeta3 is phosphorylated by CaMKII and this phosphorylation may contribute to the basal activity of PLCbeta3. PLCgamma is activated by both receptor and nonreceptor tyrosine kinases. PLCgamma forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCgamma1 on tyrosine residues 771, 783 and 1245. Phosphorylation by Syk at tyrosine 783 activates the enzymatic activity of PLCgamma1 (8). Detects total human PLCgamma1 protein levels. Does not crossreact with PLCgamma2. Species Crossreactivity: Mouse. Predicted to crossreact with rat based on sequence homology.
Immunogen
PLCG1 antibody was raised against a synthetic peptide corresponding to the C-Terminal residues of PLCG1 (Human).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
IHCIPWB
PLCG1 antibody can be used in immunohistochemistry starting at 1:50.: