Product Pathways - Ca / cAMP / Lipid Signaling
Phospho-PLCγ1 (Tyr783) Antibody #2821
|2821L||300 µl (30 western blots)||---||In Stock||---|
|2821S||100 µl (10 western blots)||---||In Stock||---|
|2821P||40 µl (4 western blots)||---||In Stock||---|
|2821||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat||Endogenous||155||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, F=Flow Cytometry
Specificity / Sensitivity
Phospho-PLCγ1 (Tyr783) Antibody detects PLCγ1 only when phosphorylated at tyrosine 783. It does not cross-react with phosphorylated PLCγ2 or other PLCs.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding tyrosine 783 of human PLCγ1. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from NIH/3T3 cells, untreated or PDGF-stimulated for the indicated times, using Phospho-PLCγ1 (Tyr783) Antibody (upper) or PLCγ1 Antibody #2822 (lower).
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).
- 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.
- Moore, A. L. et al. (2002) . J. Biol. Chem. 277, 34030-34035. Applications: Western Blotting, IC-IF.
- Krall, J.A. et al. (2011) PLoS One 6, e15945. Applications: Western Blotting.
- McPherson, V.A. et al. (2009) J Immunol 183, 4940-7. Applications: Western Blotting.
- Jung, J. et al. (2011) Oncogene 30, 2264-74. Applications: Western Blotting.
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