CPLA2-δ Rabbit Polyclonal Antibody

The phospholipase A2 enzyme family, including PLA2G4D, catalyze the hydrolysis of glycerophospholipids at the sn-2 position and then liberate free fatty acids and lysophospholipids (Chiba et al., 2004 [PubMed 14709560]) .[supplied by OMIM, Jun 2009], catalytic activity:Phosphatidylcholine + H (2) O = 1-acylglycerophosphocholine + a carboxylate., domain:The N-terminal C2 domain associates with lipid membranes and mediates its regulation by presenting the active site to its substrate in response to elevations of cytosolic Ca (2+) ., enzyme regulation:Stimulated by cytosolic Ca (2+) ., function:Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Not arachidonic acid-specific but has linoleic acid-specific activity. May play a role in inflammation in psoriatic lesions., similarity:Contains 1 C2 domain., similarity:Contains 1 PLA2c domain., subcellular location:Translocates to membrane vesicles in a calcium-dependent fashion. Translocates to perinuclear regions upon ionomycin stimulation., tissue specificity:Expressed in stratified squamous epithelia, such as those in skin and cervix, but not in other tissues. Strongly expressed in the upper spinous layer of the psoriatic epidermis, expressed weakly and discontinuously in atopic dermatitis and mycosis fungoides, and not detected in the epidermis of normal skin.