Clone REA341 recognizes the phosphoinositide phospholipase C-gamma-2 (PLC-γ2) antigen phosphorylated at tyrosine 759 (pY759). PLC-γ isoforms are mainly regulated through receptors with intrinsic tyrosine kinase activity (e.g. growth factor receptors) or receptors (such as B and T cell antigen receptors) that are linked to the activation of nonreceptor tyrosine kinases through a complex signaling network. The two isoforms of PLC-γ have distinct tissue distributions. Whereas PLC-γ1 is expressed ubiquitously, the pattern of expression of PLC-γ2 is characterized by high levels in cells of hematopoietic origin. PLC-γ2 is a transmembrane signaling enzyme that catalyzes the conversion of phosphatidyl inositol biphosphate to inositol triphosphate (IP3) and diacylglycerol (DAG) using calcium as a cofactor. It has been implicated in collagen-induced signal transduction in platelets and antigen-dependent signaling in B-lymphocytes. PLC-γ2 is regulated through activation of tyrosine kinase-linked receptors. Phosphorylation of PLC-γ2 at tyrosines 753 and 759 leads to activation of the enzyme. Homozygous disruption of PLC-γ2 results in functional and signaling disorders in a subset of cell types including B cells, platelets, and mast cells.

Additional information: Clone REA341 displays negligible binding to Fc receptors.