The gasdermin family members contain N-terminal domains that are capable of forming membrane pores to induce cytolysis, whereas the C-terminal domains of gasdermins function as inhibitors of such cytolysis through intramolecular domain association. Caspase-1 or -11 cleavage of gasdermin D is required for regulation of pyroptosis: upon protease cleavage of the gasdermin N- and C-domain linker, the disruption of the intramolecular domain interaction in the presence of lipids releases the N-domain to assemble oligomeric membrane pores that trigger cell death. Gasdermin D seems to be a key effector in the LPS-induced lethal sepsis. BioVision’s Gasdermin D (Mouse) ELISA Kit is based on the Sandwich-ELISA principle. An antibody specific for Gasdermin D has been precoated onto the 96-well microtiter plate. Standards (STD) and samples are pipetted into the wells for binding to the coated antibody. After extensive washing to remove unbound compounds, Gasdermin D is recognised by the addition of a detection antibody specific for Gasdermin D (C-terminus) (DET). After removal of excess antibody, HRP conjugated anti-Guinea Pig IgG (HRP) is added. Following a final washing, peroxidase activity is quantified using the TMB substrate. The intensity of the color reaction is measured at 450 nm after acidification and is directly proportional to the concentration of mouse Gasdermin D in the samples.