PLC-γ2 (pY759) Mouse, Alexa Fluor 488, Clone: K86-689.37, BD

Description

• Description The Phospholipase C (PLC) isozymes hydrolyze phosphatidyl inositol biphosphate to inositol triphosphate and diacylglycerol
• The former causes release of calcium from the endoplasmic reticulum, while the latter is an activator of Protein Kinase C
• Within the PLC family, PLC-γ is the only member that contains SH2 and SH3 domains
• These domains enable it to interact with protein tyrosine kinases and become enzymatically activated via phosphorylation
• It exists as two isoforms: PLC-γ1, which is ubiquitously expressed, and PLC-γ2, which is found primarily in the hematopoietic system
• PLC-γ2-null mice exhibit impaired B lymphocyte maturation and defects in Fc receptor functions
• Phosphorylation of PLC-γ2 at tyrosines 753 and 759 (Y759) is required for activation of PLC-γ2 enzyme activity
• PLC-γ2 phosphorylation at Y759 can be induced by stimulation of the B cell receptor in Ramos cell, the collagen receptor in platelets, and the T cell receptor in Jurkat cells, and it occurs downstream of Btk and BLNK in the signaling cascade of activated B cells
• The K86-689.37.73 antibody recognizes PLC-g2 phosphorylated at Y759 in the SH2-SH3 linker region
• Intracellular Staining