Product Pathways - Ca / cAMP / Lipid Signaling
Phospho-PLCγ2 (Tyr759) Antibody #3874
Reactivity Key: H=Human M=Mouse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-PLCgamma2 (Tyr759) Antibody detects endogenous levels of PLCgamma2 only when phosphorylated at tyrosine 759. The antibody does not cross-react with phosphorylated PLCgamma1.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr759 of human PLCgamma2. Antibodies are purified by protein A and peptide affinity chromatography.
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) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ and PLCε. The PLCβ subfamily includes four members, PLCβ1-4. All four members of the subfamily are activated by α- or β-γ-subunits of the heterotrimeric G-proteins (2,3).Phosphorylation is one of the key mechanisms that regulates the activity of PLC. Phosphorylation of Ser1105 by PKA or PKC inhibits PLCβ3 activity (4,5). Ser537 of PLCβ3 is phosphorylated by CaMKII, and this phosphorylation may contribute to the basal activity of PLCβ3. PLCγ is activated by both receptor and nonreceptor tyrosine kinases (6).PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783 and 1245 (7). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (8).
PLCgamma2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at tyrosines 753, 759, 1197 and 1217 is correlated with PLCgamma2 activity (9,10).
- Singer, W. D. et al. (1997) Annu. Rev. Biochem. 66, 475-509.
- Smrcka, A. V. et al. (1991) Science 251, 804-807.
- Taylor, S. J. et al. (1991) Nature 350, 516-518.
- Yue, C. et al. (1998) J. Biol. Chem. 273, 18023-18027.
- Yue, C. et al. (2000) J. Biol. Chem. 275, 30220-30225.
- Margolis, B. et al. (1989) Cell 57, 1101-1107.
- Kim, H. K. et al. (1991) Cell 65, 435-441.
- Wang, Z. et al. (1998) Mol. Cell. Biol. 18, 590-597.
- Watanabe, D. et al. (2001) J. Biol. Chem. 276, 38595-38601.
- Ozdener, F. et al. (2002) Mol. Pharmacol. 62, 672-679.
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For Research Use Only. Not For Use In Diagnostic Procedures.