The rapid protocol (RP) PathScan^® RP Cleaved Gasdermin D (Asp275) Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Gasdermin D protein when cleaved at Asp275 in a reduced assay time of 1.5 hours. This chemiluminescent ELISA, which is offered in low volume microplates, shows increased signal and sensitivity while using a smaller sample size. Incubation of cell lysates and detection antibody on the coated microwell plate forms a sandwich with cleaved Gasdermin D (Asp275) in a single step. The plate is then extensively washed and chemiluminescent reagent is added for signal development. The magnitude of light emission, measured in relative light units (RLU), is proportional to the quantity of cleaved Gasdermin D (Asp275). Learn more about all of your ELISA kit options here.

​​​​​​​*Antibodies in this kit are custom formulations specific to kit
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The PathScan^® RP Cleaved Gasdermin D (Asp275) Chemiluminescent Sandwich ELISA Kit detects endogenous levels of Gasdermin D protein only when cleaved at Asp275. The kit sensitivity is shown in Figure 1. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.

Gasdermin D (GSDMD), a member of the gasdermin family that includes GSDMA, GSDMB, and GSDMC, has been reported to have a critical role as a downstream effector of pyroptosis (1,2). Pyroptosis is a lytic type of cell death triggered by inflammasomes, multiprotein complexes assembled in response to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) that result in the activation of caspase-1 and subsequent cleavage of pro-inflammatory cytokines IL-1β and IL-18 (3). Gasdermin D was identified by two independent groups as a substrate of inflammatory caspases, caspase-1 and caspase-11/4/5, producing two fragments: GSDMD-N and GSDMD-C. Cleavage results in release of an intramolecular inhibitory interaction between the N- and C-terminal domains, allowing the N-terminal fragment GSDMD-N to initiate pyroptosis through the formation of pores on the plasma membrane (4-7).