Phospholipase A2 has been used in phospholipase assay and to determine rat renal proximal tubular segments (PTS) viability during oxygenation and hypoxia-reoxygenation.
Phospholipase A2 from bovine pancreas has been used to determine rat renal proximal tubular segments (PTS) viability during oxygenation and hypoxia-reoxygenation and to study the impact of phospholipase A2 on tubular cell triglyceride levels.
Phospholipase A2 from bovine pancreas is a calcium-dependent lipolytic enzyme.
Hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. Aggressively attacks phospholipids in membranes of intact cells.
The E.Coli derived recombinant protein contains phospholipase P00630 bee venom protein epitopes, 26-162 amino acids. Phospholipase A2 P00630 Bee Venom is fused to a 6xHis tag at C-terminus
Bee venom phospholipase A2 (PLA) is the main allergen in the bee sting allergy. Bee venom phospholipase A2 (BV-PLA2) is a hydrolytic enzyme which specifically cleaves the sn-2 acyl bond of phospholipids at the lipid/water interface. BV-PLA2 is a 14–16-kDa glycoprotein, consisting of 134 amino acids and displaying a single carbohydrate side chain at the residue Asn13. It is also held to be responsible for some systemic anaphylactic reactions in bee venom sensitized individuals. BV-PLA2 presents 3 peptide and a glycopeptide T cell epitopes, which are recognized by both allergic and non-allergic bee venom sensitized subjects. PLA is able to elicit both IgE mediated allergy and normal immunity to bee sting which usually is associated with high affinity IgG4 anti-PLA antibodies.
