Technical Data

P4074-12A
Clone Type
Monoclonal
Host
Mouse
Source
Human
Isotype
IgG1
Clone Number
MCL-3G1
Grade
Affinity Purified
Applications
E WB
Crossreactivity
Hu
Shipping Temp
Blue Ice
Storage Temp
-20°C
Mouse Anti-sPLA2 (Human Type V)
gVPLA2, Secretory Phospholipase A2 (human Group 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. This enzyme, rather than the sPLA2 (type II), is responsible for arachidonic acid mobilization leading to prostaglandin production in macrophages and mast cells. Consistent with this role, sPLA2 (type V) is associated with the golgi apparatus, nuclear envelope, and plasma membrane in murine bone marrow-derived mast cells.6 sPLA2 (type V) has been cloned from a variety of species including human, mouse, and rat. The enzyme is expressed in heart, lung, placenta, and spleen, as well as P388D1 macrophages and mast cells.

Applications
Suitable for use in Western Blot and ELISA. Other applications not tested.
Recommended Dilution
ELISA: 1:1000 Western Blot: 1:1000 Optimal dilutions to be determined by the researcher.
Storage and Stability
Lyophilized and reconstituted products are stable for 12 months after receipt at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Immunogen
Recombinant protein corresponding to human sPLA2 (Type V), W79A mutant
Form
Supplied as a lyophilized powder from PBS, pH 7.2. Reconstitute with 100ul sterile ddH2O.
Purity
Purified by Protein A affinity chromatography.
Specificity
Recognizes human sPLA2. Does not react with cPLA2, iPLA2 or sPLA2 (Type IIa).

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
1. Balboa, M.A., Balsinde, J., Winstead, M.V., et al. Novel group V phospholipase A2 involved in arachidonic acid mobilization in murine P388D1 macrophages. J. Biol. Chem. 271(50), 32381-32384 (1996).|2. Dennis, E.A. The growing phospholipase A2 superfamily of signal transduction enzymes. Trends Biochem. Sci. 22(1), 1-2 (1997).|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. J. Biol. Chem. 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. J. Biol. Chem. 271(42), 25936-25944 (1996).|5. Muñoz, N.M., Kim, K.P., Han, S.K., et al. Characterization of monoclonal antibodies specific for 14-kDa human group V secretory phospholipase A2 (hVPLA2). Hybridoma 19(2), 171-176 (2000).|6. 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. J. Biol. Chem. 274(44), 31476-31484 (1999).|7. 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. J. Biol. Chem. 269(4), 2365-2368 (1994).|8. 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).|9. 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).
USBio References
No references available
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