Product Pathways - Ca / cAMP / Lipid Signaling
Phospho-PLCγ1 (Ser1248) Antibody #4510
|W||H M R Mk||Endogenous||155||Rabbit|
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.
Specificity / Sensitivity
Phospho-PLCγ1 (Ser1248) Antibody detects PLCγ1 only when phosphorylated at Ser1248.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser1248 of human PLCγ1. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from Jurkat or COS cells, untreated or TPA/UV treated, using Phospho-PLCγ1 (Ser1248) Antibody.
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).
Phosphorylation of PLCγ1 ar Y783 by EGFR causes a conformational change of PLCγ1 that allows the interaction of its SH3 domain with Akt proline-rich motifs. This interaction results in Akt phosphorylation of PLCγ1 at S1248 by Akt (9).
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- Yue, C. et al. (1998) J. Biol. Chem. 273, 18023-18027.
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- 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.
- Wang, Y. et al. (2006) Mol. Biol. Cell 17, 2267-2277.
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For Research Use Only. Not For Use In Diagnostic Procedures.