Catalog # PX1495
phospho-PLCγ1 (Tyr-775) Peptide
Blocking Peptide
| Blocking | 1:1000 |
| ELISA | 50 ng/well |
Size 50 μg
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). 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. PLCδ is activated by both receptor and nonreceptor tyrosine kinases. PLCγ1 forms a complex with EGF and PDGF receptors, which leads to phosphorylation at tyrosine 771, 783, and 1245. In addition, antigen receptor-induced activation of PLCγ1 leads to phosphorylation at both Tyr-775 and Tyr-783. These two sites are equally important for activation of enzymatic activity.
References
Chen, P. et al. (1996) J Cell. Biol. 134:689.
Obermeier, A. et al. (1996) EMBO J. 15:73.
Western blot analysis of PLCγ1 immunoprecipitates from human jurkat cells untreated (lanes 1 & 3) or treated with pervanadate (1 mM) for 30 min (lanes 2,4,5,6). Immunoprecipitation was performed with anti-PLCγ1 (PM1561). The blots were probed with anti-PLCγ1 (lanes 1 & 2) and anti-PLCγ1 (Tyr-775) (lanes 3-6). The latter antibody was used in the presence of phospho- PLCγ1 (Tyr-775) peptide (lane 5), or unrelated phosphotyrosine peptide (lane 6).
*For more information, see UniProt Accession P19174
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains:
