Recombinant Human PLA2G1B Protein, CF

Secretory Phopholipase A₂ is an enzyme that hydrolyses the sn-2 ester bond of phospholipids and cell membranes, generating non-esterified free fatty acids and lysophospholipids (1‑3). Most secretory PLA₂s are stored in cytoplasmic granules and are released in the extracellular environment on appropriate cell activation. Thus, they are present at higher concentration in the plasma and biological fluids of patients with systemic inflammatory, autoimmune, or allergic disease, such as acute pancreatitis, rheumatoid arthritis, bronchial asthma, and allergic rhinitis. PLA2G1B has been thought to play major role in digestion of glycerophospholipids in nutrients, given its abundance in digestive organs (4). Since its expression has been observed in non-digestive organs including the lung, spleen, kidney, ovary, retina, brain, and neurons, its function may not limited to digestive role (5, 6). rhPLA2G1B has been maturated by cleaving the pro-peptide with trypsin, and the mature active form was further purified with ion-exchange column chromatograpy.