Phospho-PLCbeta3 (Ser537) (D8K2R) Rabbit mAb #29021
- WB
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 150 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser537of human PLCβ3 protein.
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).
- 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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