A major signaling mediator downstream of receptor tyrosine kinase (RTK) pathways is phospholipase C (PLC), a family of cytoplasmic proteins that cleave phospholipids to activate the subsequent signal transduction pathways. Upon activation by RTKs or G protein-coupled receptors (GPCRs), PLC cleaves the phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), which activates the calcium-dependent protein kinase C (PKC) and Ca2+ release from the endoplasmic reticulum (ER) to the cytoplasm. PKC and calcium spike in turn activate downstream effectors to mediate various cellular changes and activities. A total of 13 different PLC family members, divided into 6 classes, have been identified in humans, including β, γ, δ, ε, η, and ζ, and each has a specific tissue distribution. PLC-γ has 2 isoforms, PLC-γ1 and PLC-γ2. PLC-γ1 is expressed ubiquitously and has an essential role in growth and development, while PLC-γ2 is expressed mainly in hematopoietic cells and plays an essential role in B cell development and function.
Anti-pPLCg2 [Y759] (K86-689.37)-162Dy—50 Tests