Cell Signaling Technology

Product Pathways - Ca / cAMP / Lipid Signaling

PLCγ2 Antibody #3872

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M (R) Endogenous 150 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

PLCgamma2 Antibody detects endogenous levels of total PLCγ2 protein. This antibody does not cross-react with PLCγ1.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding the carboxy-terminus of human PLCγ2. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from Ramos (lane 1), THP1 (lane 2), U-937 (lane 3) cells and mouse spleenocytes (lane 4), using PLCγ2 Antibody.

Western Blotting

Western Blotting

Western blot analysis of extracts from NIH/3T3 (lanes 1, 3, 5) and Ramos (lanes 2, 4, 6) cells, using PLCγ1 Antibody #2822 (lanes 1 and 2), PLCgamma2 Antibody (lanes 5 and 6) or both antibodies (lanes 3 and 4). Results show that PLCγ2 Antibody is specific to the 150 kDa PLCγ2 band detected in Ramos cells, while PLCγ1 Antibody #2822 is specifc to the 160 kDa PLCγ1 band detected in both Ramos and NIH/3T3 cells.

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) (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).

PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197 and 1217 is correlated with PLCγ2 activity (9,10).

  1. Singer, W. D. et al. (1997) Annu. Rev. Biochem. 66, 475-509.
  2. Smrcka, A. V. et al. (1991) Science 251, 804-807.
  3. Taylor, S. J. et al. (1991) Nature 350, 516-518.
  4. Yue, C. et al. (1998) J. Biol. Chem. 273, 18023-18027.
  5. Yue, C. et al. (2000) J. Biol. Chem. 275, 30220-30225.
  6. Margolis, B. et al. (1989) Cell 57, 1101-1107.
  7. Kim, H. K. et al. (1991) Cell 65, 435-441.
  8. Wang, Z. et al. (1998) Mol. Cell. Biol. 18, 590-597.
  9. Watanabe, D. et al. (2001) J. Biol. Chem. 276, 38595-38601.
  10. Ozdener, F. et al. (2002) Mol. Pharmacol. 62, 672-679.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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