PLCγ1 Antibody #2822
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 155 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
PLCγ1 Antibody detects endogenous levels of total PLCγ1 protein. This antibody does not cross-react with PLCγ2.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy-terminal residues of human PLCγ1. Antibodies are purified by protein A and peptide affinity chromatography.
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 1248 (7). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (8).
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 1248 (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, 804-7.
- Taylor, S.J. et al. (1991) Nature 350, 516-8.
- Yue, C. et al. (1998) J Biol Chem 273, 18023-7.
- Yue, C. et al. (2000) J Biol Chem 275, 30220-5.
- Margolis, B. et al. (1989) Cell 57, 1101-7.
- Kim, H.K. et al. (1991) Cell 65, 435-41.
- Wang, Z. et al. (1998) Mol Cell Biol 18, 590-7.
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