For immunochemical detection of sPLA2 (human Type V)
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sPLA2 (human Type V) Monoclonal Antibody (Clone MCL-3G1)

Item No. 160510

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • gVPLA2
  • Secretory Phospholipase A2 (human Group V)
Immunogen
Recombinant human sPLA2 (Type V), W79A mutant
Clone Designation
MCL-3G1
Formulation (Request formulation change)
100 µg of protein A-purified antibody
Storage Buffer
PBS, pH 7.2, when reconstituted in 100 μl double distilled water
Host
Mouse
Isotype
IgG1
Applications
ELISA and WB
Cross Reactivity
(-) cPLA2(-) iPLA2(-) sPLA2 (Type IIa)
Species Reactivity
(+) Human
UniProt Accession №
P39877
Origin
Animal/Mouse
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    100 µg

    $347

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    Product Description

    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.2,3,4,5 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.7,8,9 The enzyme is expressed in heart, lung, placenta, and spleen, as well as P388D1 macrophages and mast cells.2,3,9

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description 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. The Journal of Biological Chemisty 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. 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. 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. The Journal of Biological Chemisty 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. The Journal of Biological Chemisty 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).

    Product Citations

    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).