Recombinant Human Gasdermin-D (GSDMD) N-terminal Fragment (residues 1-90) is a high-purity protein product designed for studying pyroptosis and inflammasome signaling. This fragment encompasses the critical N-terminal domain responsible for membrane pore formation, offering researchers a stable and soluble tool for structural, biochemical, and functional assays in innate immunity and host-pathogen interactions.

Gasdermin-D is a key pore-forming protein in human host defense, playing a central role in pyroptosis—a form of inflammatory cell death—in response to pathogens and danger signals. The full-length protein is cleaved by inflammatory caspases (e.g., CASP1, CASP4, CASP5) to release the N-terminal fragment (GSDMD-NT), which translocates to the plasma membrane, binds phosphoinositides, and forms oligomeric pores. These pores facilitate the release of mature interleukins (e.g., IL1B, IL18) and trigger pyroptosis, contributing to antimicrobial defense and immune regulation. The protein localizes to t