sPLA₂ (human, recombinant Type V)

Phospholipase A₂ (PLA₂) catalyzes the hydrolysis of fatty acids at the sn-2 position of glycerophospholipids. PLA₂ (Type V) is a secretory PLA₂ (sPLA₂) of approximately 14 kDa and is one of the isoforms in the growing list of the PLA₂ enzyme family.¹ This enzyme, rather than the sPLA₂ (Type II), is responsible for arachidonic acid mobilization leading to prostaglandin production in macrophages and mast cells.^2,3,4 Consistent with this role, sPLA₂ (Type V) is associated with the golgi apparatus, nuclear envelope, and plasma membrane in mouse bone marrow-derived mast cells.⁵ sPLA₂ (Type V) has been cloned from a variety of species including human, mouse, and rat.^6,7,8 The enzyme is expressed in heart, lung, placenta, and spleen, as well as P388D1 macrophages and mast cells.^2,3,8 The specific activity of Cayman’s sPLA₂ (human, recombinant Type V) was established using 1,2-bis(heptanoylthio) Glycerophosphocholine (Cayman Item No. 62235) as the substrate. The reaction was inhibited by thioetheramide-PC (Cayman Item No. 62750).

WARNING This product is not for human or veterinary use.

1. Balsinde, J., Winstead, M.V., and Dennis, E.A. Phospholipase A₂ regulation of arachidonic acid mobilization. FEBS Lett. 531(1), 2-6 (2002).

2. Balboa, M.A., Balsinde, J., Winstead, M.V., et al. Novel group V phospholipase A₂ involved in arachidonic acid mobilization in murine P388D1 macrophages. The Journal of Biological Chemisty 271(50), 32381-32384 (1996).

3. Reddy, S.T., Winstead, M.V., Tischfield, J.A., et al. Analysis of the secretory phospholipase A₂ that mediates prostaglandin production in mast cells. The Journal of Biological Chemisty 272(21), 13591-13596 (1997).

4. Bingham, C.O., III, Murakami, M., Fujishima, H., et al. A heparin-sensitive phospholipase A₂ and prostaglandin endoperoxide synthase-2 are functionally linked in the delayed phase of prostaglandin D₂ generation in mouse bone marrow-derived mast cells. The Journal of Biological Chemisty 271(42), 25936-25944 (1996).

5. Bingham, C.O., III, Fijneman, R.J.A., Friend, D.S., et al. Low molecular weight group IIA and group V phospholipase A₂ enzymes have different intracellular locations in mouse bone marrow-derived mast cells. The Journal of Biological Chemisty 274(44), 31476-31484 (1999).

6. Chen, J., Engle, S.J., Seilhamer, J.J., et al. Cloning and recombinant expression of a novel human low molecular weight Ca²⁺-dependent phospholipase A₂. The Journal of Biological Chemisty 269(4), 2365-2368 (1994).

7. Tischfield, J.A., Xia, Y.R., Shih, D.M., et al. Low-molecular-weight, calcium-dependent phospholipase A₂ genes are linked and map to homologous chromosome regions in mouse and human. Genomics 32(3), 328-333 (1996).

8. Chen, J., Engle, S.J., Seilhamer, J.J., et al. Cloning, expression and partial characterization of a novel rat phospholipase A₂. Biochim. Biophys. Acta 1215(1-2), 115-120 (1994).

Takahama, M., Wolfe, K.S., Richey, G., et al. Secreted phospholipase PLA2G5 acts as a hemolytic factor in sepsis. J. Clin. Invest. 136(9), e195001 (2026).