Phospho-Phospholipase Cγ1/PLC-γ-1 (Tyr783) Antibody [J4J15]

Application: Reactivity: Mouse, Human

Lane 1: Jurkat, Lane 2: Jurkat (pervanadate, 50mM, 5 min), Lane 3: Jurkat (pervanadate, 50mM, 5 min; alkaline phosphatase treated)

Usage Information

Dilution
WB1:100000 - 1:200000 IF1:100

Application
WB, IF

Reactivity
Mouse, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
148 kDa 149 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Jurkat cells (Pervanadate, 1mM, 30 min); Jurkat cells (Pervanadate, 50mM, 5 min)
Negative Control	Jurkat cells

Datasheet & SDS

Biological Description

Specificity
Phospho-Phospholipase Cγ1/PLC-γ-1 (Tyr783) Antibody [J4J15] detects endogenous levels of total Phospholipase Cγ1/PLC-γ-1 protein only when it is phosphorylated at Tyr783.

Clone
J4J15

Synonym(s)
PLC1; PLCG1; PLC-148; Phosphoinositide phospholipase C-gamma-1; Phospholipase C-II; Phospholipase C-gamma-1; PLC-II; PLC-gamma-1

Background
Phospho-Phospholipase Cγ1 (Tyr783), the activated form of PLC-γ1, is a pivotal effector in receptor tyrosine kinase (RTK) signaling. Upon RTK stimulation, Tyr783 of PLC-γ1 becomes phosphorylated, typically by kinases such as EGFR, PDGFR, Syk, or Src family members. This phosphorylation event triggers a conformational change, relieving autoinhibition imposed by the split SH2-SH2-SH3 domains that otherwise clamp the catalytic core. The phosphorylated Tyr783 in the SH2 linker binds intramolecularly to the cSH2 domain, displacing it from the C2 core interface and exposing the active site for membrane docking and catalysis. PLC-γ1 features an N-terminal PH domain for PIP2 membrane recruitment, a catalytic TIM barrel (X-Y domains), EF hands and a C2 domain for Ca2+/lipid sensing, and regulatory SH2-SH2-SH3 domains. Once activated, PLC-γ1 hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). These second messengers drive intracellular calcium release and protein kinase C (PKC) activation, propagating downstream signaling. The high-affinity cSH2-pTyr783 interaction outcompetes autoinhibitory contacts, stabilizing an open, catalytically active conformation and amplifying IP3/DAG production. This sustains Ca2+ oscillations, PKC/ERK crosstalk, cytoskeletal remodeling, gene expression, and chemotaxis, especially in immune cells. Rapid dephosphorylation of Tyr783 ensures timely signal termination. Phospho-PLCγ1 is indispensable for platelet aggregation, T and B cell activation, and RTK-driven cell proliferation. Aberrant Tyr783 phosphorylation can cause immune disorders (e.g., SCID from gain-of-function mutations), hematologic malignancies via hyperactive PLC signaling, and drive invasion and angiogenesis in solid tumors.

Background

Phospho-Phospholipase Cγ1 (Tyr783), the activated form of PLC-γ1, is a pivotal effector in receptor tyrosine kinase (RTK) signaling. Upon RTK stimulation, Tyr783 of PLC-γ1 becomes phosphorylated, typically by kinases such as EGFR, PDGFR, Syk, or Src family members. This phosphorylation event triggers a conformational change, relieving autoinhibition imposed by the split SH2-SH2-SH3 domains that otherwise clamp the catalytic core. The phosphorylated Tyr783 in the SH2 linker binds intramolecularly to the cSH2 domain, displacing it from the C2 core interface and exposing the active site for membrane docking and catalysis. PLC-γ1 features an N-terminal PH domain for PIP2 membrane recruitment, a catalytic TIM barrel (X-Y domains), EF hands and a C2 domain for Ca2+/lipid sensing, and regulatory SH2-SH2-SH3 domains. Once activated, PLC-γ1 hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). These second messengers drive intracellular calcium release and protein kinase C (PKC) activation, propagating downstream signaling. The high-affinity cSH2-pTyr783 interaction outcompetes autoinhibitory contacts, stabilizing an open, catalytically active conformation and amplifying IP3/DAG production. This sustains Ca2+ oscillations, PKC/ERK crosstalk, cytoskeletal remodeling, gene expression, and chemotaxis, especially in immune cells. Rapid dephosphorylation of Tyr783 ensures timely signal termination. Phospho-PLCγ1 is indispensable for platelet aggregation, T and B cell activation, and RTK-driven cell proliferation. Aberrant Tyr783 phosphorylation can cause immune disorders (e.g., SCID from gain-of-function mutations), hematologic malignancies via hyperactive PLC signaling, and drive invasion and angiogenesis in solid tumors.

References
https://pubmed.ncbi.nlm.nih.gov/35367415/ https://pubmed.ncbi.nlm.nih.gov/31889510/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%