Cleaved Gasdermin B (Lys229) (E1Y2E) Rabbit mAb #64436

The gasdermin family, which includes GSDMA, GSDMB, GSDMC, GSDMD, and GSDME, has been shown to play a role in inflammation and cell death. Gasdermin D 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).

Gasdermin B (GSDMB) has been reported to be upregulated in several tumor types, and in breast cancer, has been associated with metastasis and poor prognosis (8,9). In addition, Gasdermin B has been associated with immune disorders, including asthma (10,11). Gasdermin B expression has also been found in the lung epithelium associated with asthma. Gasdermin B can also have a role in pyroptosis as it was found to activate caspase-4 and promote Gasdermin D cleavage (12). Cleavage and the pore-forming ability of Gasdermin B are induced by Granzyme A secreted by cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells (13).