For the measurement of sPLA2 activity
Features
  • Measure sPLA2 activity
  • Assay 46 samples in duplicate
  • Measure sPLA2 activity down to 0.02 U/ml
  • Plate-based colorimetric measurement (405-414 nm)
Technical Support & Resources

Visit our FAQ

Contact Us

Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888

Request Technical Support

Technical Support Request

To streamline the process attach the appropriate questionnaire to your inquiry.

Download IHC QuestionnaireDownload WB Questionnaire

View Our Privacy Statement for details on how we use and protect your data. In addition, this site is protected by hCaptcha and its Privacy Policy and Terms of Service apply.

sPLA2 Assay Kit

Item No. 765001

Kit Booklet (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Secretory Phospholipase A2 (Type IIA) Assay Kit
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
Recommended Products

Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

    96 wells

    $468

    Add
    Lipid Resource Center
    Discover Products & Resources for Lipid Research
    • High-purity lipid standards
    • Lipid roles in biology
    • Lipids in health & disease
    • Lipids for pharmaceutical development
    • Protocols, advice, & resources
    EXPLORE NOW
    Product Description

    Phospholipase A2 (PLA2) catalyzes the hydrolysis of phospholipids at the sn-2 position yielding a free fatty acid and a lysophospholipid.1 The release of arachidonic acid from membrane phospholipids by PLA2 is believed to be a key step in the control of eicosanoid production within the cell.2 The Cayman Chemical secretory PLA2 (sPLA2) Assay kit provides an accurate and convenient method for measurement of sPLA2 activity. This assay uses the 1,2-dithio analog of diheptanoyl phosphatidylcholine which serves as a substrate for most PLA2s (for example, bee and cobra venoms, pancreatic, etc.) with the exception of cytosolic PLA2.3,4 Upon hydrolysis of the thio ester bond at the sn-2 position by PLA2, free thiols are detected using DTNB (5,5-dithio-bis-(2-nitrobenzoic acid)).

    Needed but not supplied: Please download the kit booklet to verify if UltraPure Water (Milli-Q or equivalent) or any other components are needed for this assay.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Dennis, E.A. Phospholipases. The Enzymes XVI, (1983).

    2. Dennis, E.A. Diversity of group types, regulation, and function of phospholipase A2. The Journal of Biological Chemisty 269(18), 13057-13060 (1994).

    3. Hendrickson, H.S., Hendrickson, E.K., and Dybvig, R.H. Chiral synthesis of a dithiolester analog of phosphatidylcholine as a substrate for the assay of phospholipase A2. J. Lipid Res. 24(11), 1532-1537 (1983).

    4. Reynolds, L.J., Hughes, L.L., and Dennis, E.A. Analysis of human synovial fluid phospholipase A2 on short chain phosphatidylcholine-mixed micelles: Development of a spectrophotometric assay suitable for a microtiterplate reader. Anal. Biochem. 204(1), 190-197 (1992).

    Product Citations

    Zhang, T., Yu, W., Cheng, X., et al. Up-regulated PLA2G10 in cancer impairs T cell infiltration to dampen immunity. Sci. Immunol. 9, eadh2334 (2024).

    Jaiswal, A., Rehman, R., Dutta, J., et al. Cellular distribution of secreted phospholipase A2 in lungs of IPF patients and its inhibition in bleomycin-induced pulmonary fibrosis in mice. Cells 12(7), 1044 (2023).

    Hou, S., Xu, T., Xu, J., et al. Structural basis for functional selectivity and ligand recognition revealed by crystal structures of human secreted phospholipase A2 group IIE. Sci. Rep. 7(1), 10815 (2017).

    Hou, S., Bai, J., Chen, C., et al. The atypical binding mechanism of second calcium on phospholipase A2 group IIE. Biochem. Biophys. Res. Commun. 557, 267-272 (2021).

    Debono, J., Cochran, C., Kruruppu, S., et al. Canopy venom: Proteomic comparison among new world arboreal pit-viper venoms. Toxins (Basel) 8(7), E210 (2016).

    Zhang, Y., Xu, T., Chen, Q., et al. Expression, purification, and refolding of active human and mouse secreted group IIE phospholipase A2. Protein Expr. Purif. 80(1), 68-73 (2011).