Product Pathways - Ca / cAMP / Lipid Signaling
PLCγ1 (D9H10) XP® Rabbit mAb #5690
PhosphoSitePlus® protein, site, and accession data: PLCG1
| Applications | Reactivity | Sensitivity | MW (kDa) | Isotype |
|---|---|---|---|---|
| W IP IHC-P | H M R Mk | Endogenous | 150 kDa | Rabbit IgG |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
IHC-P=Immunohistochemistry (Paraffin)
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.
Protocols
Specificity / Sensitivity
PLCγ1 (D9H10) XP® Rabbit mAb recognizes endogenous levels of total PLCγ1 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu1220 of human PLCγ1 protein.
Western Blotting
Western blot analysis of extracts from HeLa cells, either mock-transfected or transfected for 48 hours with SignalSilence™ PLCγ1 siRNA I #6293 or siRNA II #6254, using PLCγ1 (D9H10) XP® Rabbit mAb.
Western Blotting
Western blot analysis of extracts from various cell lines using PLCγ1 (D9H10) XP® Rabbit mAb.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using PLCγ1 (D9H10) XP® Rabbit mAb.
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. Phosphorylation is one of the key mechanisms that regulate the activity of PLC. PLCγ is activated by both receptor and non-receptor tyrosine kinases (2). PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783, and 1245 (3). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (4). PLCγ2 is engaged in antigen-dependent signaling in B cells and collagen-dependent signaling in platelets. Phosphorylation by Btk or Lck at Tyr753, 759, 1197, and 1217 is correlated with PLCγ2 activity (5,6).
- Singer, W.D. et al. (1997) Annu Rev Biochem 66, 475-509.
- 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.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.