Phospho-PLCγ2 (Tyr1217) (E2U1K) Rabbit mAb #54442
- WB
- IP
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 150 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Flow Cytometry (Fixed/Permeabilized) | 1:100 - 1:400 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
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).
PLCgamma2 is engaged in antigen-dependent signaling in B cell and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at tyrosines 753, 759, 1197 and 1217 is correlated with PLCgamma2 activity (9,10).
- 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.
- Watanabe, D. et al. (2001) J Biol Chem 276, 38595-601.
- Ozdener, F. et al. (2002) Mol Pharmacol 62, 672-9.
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