Cell Signaling Technology

Product Pathways - Ca / cAMP / Lipid Signaling

PLCbeta3 Antibody #2482

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

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

Protocols

Specificity / Sensitivity

PLCbeta3 Antibody detects endogenous levels of total PLCbeta3 protein. The antibody does not cross-react with PLCbeta1, PLCbeta2 or PLCbeta4.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding residues surrounding carboxy-terminal residues of human PLCbeta3. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa cells, untreated or PMA-treated for the indicated times, using PLCbeta3 Antibody.

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).

  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.

Application References

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Companion Products

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

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