Datasheet

Biological Description

Specificity	Phospho-PLCγ1 (Tyr783) Antibody [C6N17] detetcs endogenous levels of PLCγ1 protein only when phosphorylated at Tyr783.
Background	Phospho-PLCγ1 (Tyr783) represents the activated form of PLCγ1, a receptor-proximal signaling enzyme that hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP₂) to generate the second messengers IP₃ and DAG, thereby activating protein kinase C (PKC) and mobilizing intracellular Ca²⁺. Structurally, PLCγ1 is composed of a catalytic core (X–Y domain) regulated by an autoinhibitory X–Y linker containing multiple domains: pleckstrin homology (PH), Src homology 2 (nSH2, cSH2), and SH3. In its basal state, the cSH2 domain interacts with the C2 domain of the catalytic core, physically blocking membrane access. PLCγ1 is broadly expressed in mammalian tissues, particularly in hematopoietic and epithelial cells, where it transduces signals downstream of receptor tyrosine kinases, immune receptors, and growth factor receptors. Phosphorylation at Tyr783, mediated by receptor-associated kinases, is the hallmark event that relieves autoinhibition: the phosphorylated Tyr783 acts as an intramolecular ligand that binds to the cSH2 domain, displacing it from the catalytic core and allowing exposure of a hydrophobic ridge required for membrane insertion and catalysis. This phosphorylation is essential because it locks PLCγ1 into its active conformation, stabilizes its interaction with the plasma membrane, and ensures robust propagation of receptor signaling, with dysregulated phospho-PLCγ1 implicated in oncogenesis and aberrant immune activation.

Specificity

Phospho-PLCγ1 (Tyr783) Antibody [C6N17] detetcs endogenous levels of PLCγ1 protein only when phosphorylated at Tyr783.

Background

Phospho-PLCγ1 (Tyr783) represents the activated form of PLCγ1, a receptor-proximal signaling enzyme that hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP₂) to generate the second messengers IP₃ and DAG, thereby activating protein kinase C (PKC) and mobilizing intracellular Ca²⁺. Structurally, PLCγ1 is composed of a catalytic core (X–Y domain) regulated by an autoinhibitory X–Y linker containing multiple domains: pleckstrin homology (PH), Src homology 2 (nSH2, cSH2), and SH3. In its basal state, the cSH2 domain interacts with the C2 domain of the catalytic core, physically blocking membrane access. PLCγ1 is broadly expressed in mammalian tissues, particularly in hematopoietic and epithelial cells, where it transduces signals downstream of receptor tyrosine kinases, immune receptors, and growth factor receptors. Phosphorylation at Tyr783, mediated by receptor-associated kinases, is the hallmark event that relieves autoinhibition: the phosphorylated Tyr783 acts as an intramolecular ligand that binds to the cSH2 domain, displacing it from the catalytic core and allowing exposure of a hydrophobic ridge required for membrane insertion and catalysis. This phosphorylation is essential because it locks PLCγ1 into its active conformation, stabilizes its interaction with the plasma membrane, and ensures robust propagation of receptor signaling, with dysregulated phospho-PLCγ1 implicated in oncogenesis and aberrant immune activation.

Usage Information

Application

WB, IP, FCM

Dilution

WB	IP	FCM
1:1000	1:50	1:100 - 1:400

Reactivity

Human, Mouse

Source

Rabbit Monoclonal Antibody

MW

155 kDa

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

Exprimental Methods

References

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

Phospho-PLCγ1 (Tyr783) Antibody [C6N17]

Biological Description

Usage Information

References

Application Data