PLCγ1 (Tyr-775), Phosphospecific Antibody

Product Specifications

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) . At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ, and PLCε. Phosphorylation is one of the key mechanisms that regulates 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.

Synonyms

Phospholipase C gamma1, phosphodiesterase

Swiss Prot

P19174

Modification Site

Tyr-775

Host

Rabbit

Cross Reactivity

Human, Mouse, Rat

Target

PLCγ1 (Tyr-775)

Clonality

Polyclonal

Isotype

IgG

Conjugation

Unconjugated

Source

PLCγ1 (Tyr-775) synthetic peptide (coupled to carrier protein) corresponding to amino acids around tyrosine 775 in human PLCγ1.

Applications

WB, IP

Purification

Antigen Affinity purification

Dilution

WB (1:300-5000), IP (1-2ug)

Buffer

PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Modification

Phosphorylation

Storage Conditions

Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Specificity

This antibody was cross-adsorbed to a non-specific phospho-tyrosine peptide then affinity-purified using phospho-PLCγ1 (Tyr-775) peptide. The antibody detects a 150 kDa* protein in human Jurkat and A431 cells treated with pervanadate, but is not observed in untreated cells. This sequence has high homology to the conserved site in rat and mouse PLCγ1, and has low homology to PLCγ2.