Anti-Phospholipase A2 Antibody, clone CH-7

Phospholipases hydrolyze phosphoglycerides to form smaller compounds which often serve as critical second messengers. Phospholipase A2 (PLA2) hydrolyzes phosphatidylcholine to produce lysophosphatidylcholine, a second messenger involved in cell proliferation, adhesion, T-cell activation, and smooth muscle cell contractility. PLA2 isoforms include membrane-associated, Ca2+-independent forms, cytosolic, Ca2+-dependent forms, and secretory forms. PLC catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate, to generate inositol (1,4,5) trisphosphate (IP3) and diacylglycerol (DAG), leading to Ca2+ release and PKC activation, respectively. At least four types of PLC have been identified. PLCbeta, is activated by G-Protein-Coupled Receptors (GPCRs) and heterotrimeric G-Proteins. Mechanisms of PLCdelta activation are unclear, but may also involve GPCRs. PLCgamma, is activated by receptor tyrosine kinases, and appears essential for signaling by the PDGF Receptor. PLCepsilon is a Guanine Nucleotide Exchange factor (GEF) for the small G-Protein Ras. PLD activity is up-regulated when cells are stimulated by hormones, growth factors or other extracellular signals. Two distinct PLDs, PLD1 and PLD2, have been identified. PLD hydrolyzes phosphatidylcholine to release phosphatidic acid, which is associated with a number of cellular responses including regulated secretion, mitogenesis and cytoskeletal changes.