Anti-Caspase-4 Antibody

Inflammatory caspase that acts as an essential effector of the NLRP3 and NLRP6 inflammasomes by mediating lipopolysaccharide (LPS)-induced pyroptosis (PubMed:7797510, PubMed:23516580, PubMed:26375003, PubMed:32109412). Thiol protease that cleaves a tetrapeptide after an Asp residue at position P1: catalyzes cleavage of CGAS, GSDMD and IL18 (PubMed:7797510, PubMed:15326478, PubMed:23516580, PubMed:26375003, PubMed:28314590, PubMed:32109412). Required for innate immunity to cytosolic, but not vacuolar, bacteria (By similarity). Plays a key role in NLRP3-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS (PubMed:26508369, PubMed:22246630, PubMed:23516580, PubMed:24879791, PubMed:25119034, PubMed:26173988, PubMed:26174085, PubMed:25964352). Activated by direct binding to LPS without the need of an upstream sensor (PubMed:25119034). Involved in NLRP6 inflammasome-dependent activation in response to lipoteichoic acid (LTA), a cell-wall component of Gram-positive bacteria, which leads to CASP1 activation and IL1B and IL18 secretion (PubMed:33377178). Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, followed by IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators (PubMed:26375003, PubMed:32109412). Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection: in later stages of the infection, LPS from cytosolic Salmonella triggers CASP4 activation, which catalyzes cleavage of GSDMD, resulting in pyroptosis of infected cells and their extrusion into the gut lumen, as well as in IL18 secretion (PubMed:25121752, PubMed:26375003, PubMed:25964352, PubMed:34671164, PubMed:32109412). Cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP4 that rUniProtKB:P70343, PubMed:15123740, PubMed:15326478, PubMed:22246630, PubMed:23516580, PubMed:23661706, PubMed:24879791, PubMed:25119034, PubMed:25121752, PubMed:25964352, PubMed:26173988, PubMed:26174085, PubMed:26375003, PubMed:26508369, PubMed:28314590, PubMed:32109412, PubMed:33377178, PubMed:34671164, PubMed:7743998, PubMed:7797510, PubMed:7797592}.; (Microbial infection) In response to the Td92 surface protein of the periodontal pathogen T.denticola, activated by cathepsin CTSG which leads to production and secretion of IL1A and pyroptosis of gingival fibroblasts. {PubMed:29077095}.

Immunoblotting: use at 1ug/mL. <br><br>Positive control: Ramos cell lysate. <br><br>Immunohistochemistry: use at 2ug/mL. <br><br>These are recommended concentrations. <br><br>Enduser should determine optimal concentrations for their applications.

Caspases are a family of cysteine proteases. Caspase-4 was initially identified as a homologous protein to Caspase-1 and the C. elegans Ced-3 which could induce apoptosis in transfected cells. More recent studies have shown that it can be activated by ER stress and has been suggested to be involved in multiple neuronal pathologies such as Alzheimer's disease.