Positive control for cPLA2. The optimal molecular weight for 264.7 RAW cells is ~100 kDa without proteolysis. The full range for cPLA2 has been reported to be ~80-100 kDa.
Phospholipase A2 (PLA2) enzymes hydrolyze the acyl group from the sn-2 position of glycerophospholipids. Both products of the reaction, the fatty acid and the lysophospholipid, may act as second messengers. PLA2 enzymes are classified based on their molecular size, substrate specificity, amino acid sequence and disulfide bond pattern. Type II PLA2 enzymes are well characterized secretory enzymes by their disulfide bonds, small size, dependence on Ca2+, and the lack of preference for arachidonic acid over other acyl groups at the sn-2 position. Type IV PLA2 are very distinct in that they are localized in the cytosol, are larger and prefer arachidonic acid at the sn-2 position. Some type IV PLA2 enzymes are Ca2+-dependent, others are not. Recently, several additional members of the PLA2 superfamily have been identified, leading to the addition of classes V (secretory), VI (80 kDa inducible), VII and VIII (both of which are Ca2+-independent and specific for platelet activating factor) and IX (secretory). Although the importance of these enzymes in eicosanoid metabolism signal transduction is not questioned, much remains to be learned regarding the regulation of these enzymes and the pathophysiological roles of each.