Anti-phospho-PLCG1 (Tyr783)(P40-465R)
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Description :Rabbit Polyclonal Antibody
Species :
Tag :
Expression System:
Sequence :
Specificity :Recognizes the PLCG1 protein phosphorylated at tyrosine 783
Cited Applications :WB
Cross Reactivity :Human, Mouse and Rat
Host / Isotype / Clone# :Rabbit, IgG
Immunogen :Synthetic phospho-peptide corresponding to amino acid residues surrounding Tyr783
Purification :Affinity chromatography
Stability :Store at 4oC (add 0.1% NaN3) for several months, and at -20oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Sample Data :Western blot analysis of extracts from A431 cells untreated or treated with EGF (200ng/ml, 10min) using PLCG1 antibody (lanes 1 and 2) and anti-phospho-PLCG1 (Tyr783) antibody (lanes 3 and 4).
Scientific Background :Phospholipase C gamma 1 (PLCG1) plays an important role in the intracellular transduction of messages from active receptor-mediated tyrosine kinases. PLCG1 catalyzes the formation of the second-messenger molecules inositol 1, 4, 5-trisphosphate and diacylglycerol from phosphatidylinositol 4, 5-bisphosphate. PLCG1 is a substrate for heparin-binding growth factor 1 activated tyrosine kinase. PLCG1 inhibits growth factor receptor-mediated invasion of breast and prostate tumor cells and is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE (1). PLCG1 is phosphorylated at Tyr771/783/1245 upon interaction with EGF and PDGF (2) and the Tyr783 of PLCG1 is phosphorylated directly by SYK (3).
References :
1. Ye, K. et al: Phospholipase C-gamma-1 is a physiological guanine nucleotide exchange factor for the nuclear GTPase PIKE. Nature 415: 541-544, 2002.
2. Kim H K. et al: PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254. Cell. 1991 May 3;65(3):435-41.
3. Wang Z. et al: Requirement for phospholipase c-gamma1 enzymatic activity in growth factor-induced mitogenesis. Mol Cell Biol. 1998 Jan;18(1):590-7.
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Research Areas :Cancer, Neurobiology, Inflammation, Metabolic Disorder, Cardiovascular Disease, PKA/PKC Pathway