Clone REA488 recognizes the human phosphoinositide phospholipase C-γ-2 (PLC-γ2) antigen regardless of phosphorylation status. 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 non-receptor 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. 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 REA488 displays negligible binding to Fc receptors.