GSDMD Recombinant Rabbit mAb (S-3035)

Gasdermin D (GSDMD) is a crucial protein within the gasdermin family, playing a key role in executing pyroptosis, a form of lytic, inflammatory cell death. The full-length GSDMD protein is inactive and consists of a 31 kD N-terminal pore-forming domain and a 22 kD C-terminal suppression domain. Upon activation by caspases such as caspase-1, -4, -5, or -11, the interdomain linker is cleaved, releasing the N-terminal fragment (GSDMD-NT) from the inhibitory C-terminal domain. The freed GSDMD-NT translocates to the plasma membrane, oligomerizes, and forms pores with an inner diameter of approximately 10–14 nm, leading to cell lysis, cytokine release (such as IL-1β and IL-18), and disruption of ion and water balance. This pore formation is a critical step in mediating inflammation and immune responses. GSDMD is also implicated in various diseases, including sepsis, myocardial ischemia/reperfusion injury, and certain cancers. Research on selective GSDMD inhibitors is ongoing, aiming to block pyroptosis and reduce inflammation in pathological conditions.