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Reference: 560131-96

The COX (ovine/human) Inhibitor Screening Assay directly measures PGF2α produced by SnCl2 reduction of COX-derived PGH2. The prostanoid product is quantified via ELISA using a broadly specific antibody that binds to all the major PG compounds. Thus, the Cayman COX Assay is more accurate and reliable than an assay based on peroxidase inhibition. Cayman’s COX Inhibitor Screening Assay includes both ovine COX-1 and human recombinant COX-2 enzymes in order to screen isozyme-specific inhibitors. This assay is an excellent tool which can be used for general inhibitor screening, or to eliminate false positive leads generated by less specific methods.

Reference: 600007-1920

PGD2 is synthesized by H-PGDS in mast cells and is released in large quantities during allergic and asthmatic anaphylaxis. H-PGDS is therefore a key target for development of selective, potent inhibitors for therapeutic use against these diseases. Cayman’s H-PGDS FP-Based Inhibitor Screening Assay provides a rapid, accurate assay for screening H-PGDS inhibitors. In this assay, a H-PGDS inhibitor-fluorescein conjugate serves as a specific fluorescent probe for the enzyme. Displacement of the probe by any unlabeled H-PGDS inhibitor leads to a decrease in the fluorescence polarization (FP) state of the probe, providing a direct signal for binding of the inhibitor to the active site of the enzyme. This assay is robust (Z' of 0.75) and eliminates the need for the traditional multistep assay that requires the use of highly unstable PGH2. The assay has been validated using several known inhibitors of H-PGDS with IC50 values ranging from nanomolar to millimolar concentrations.

Reference: 600007-384

PGD2 is synthesized by H-PGDS in mast cells and is released in large quantities during allergic and asthmatic anaphylaxis. H-PGDS is therefore a key target for development of selective, potent inhibitors for therapeutic use against these diseases. Cayman’s H-PGDS FP-Based Inhibitor Screening Assay provides a rapid, accurate assay for screening H-PGDS inhibitors. In this assay, a H-PGDS inhibitor-fluorescein conjugate serves as a specific fluorescent probe for the enzyme. Displacement of the probe by any unlabeled H-PGDS inhibitor leads to a decrease in the fluorescence polarization (FP) state of the probe, providing a direct signal for binding of the inhibitor to the active site of the enzyme. This assay is robust (Z' of 0.75) and eliminates the need for the traditional multistep assay that requires the use of highly unstable PGH2. The assay has been validated using several known inhibitors of H-PGDS with IC50 values ranging from nanomolar to millimolar concentrations.