Anti-NLRP1/NALP1 (NAC-delta)

This antibody detects NLRP1, human NLRP1 is a 1473 amino acid protein. NLRP1, a member of NALP CLR subfamily, has an N-terminal pyrin domain (PYD), followed by an NBD, LRR, and a C-terminal CARD domain. NLRP1 is a component of both the inflammasome and apoptosome, suggesting that NLRP1 has important roles in both inflammation and apoptosis. The N-terminal domain consists of transactivation, CARD, Pyrin or BIR domains, or in some cases is undefined. The CLR  family, also known as the NOD family, has its ancient roots in the plant kingdom and is related to the disease resistance (R) gene family that mediates plant immune responses.However, multiple splice variants encoding distinct NLRP1 isoforms with varying amino acid lengths have been described and thus the molecular weight detected may vary depending on the isoform(s) expressed. Protein function: As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP1, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu. Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (PubMed:22665479, PubMed:17418785). May be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner (PubMed:18511561). Contrary to its mouse ortholog, not activated by Bacillus anthracis lethal toxin (PubMed:19651869). It is unclear whether isoform 2 is involved in inflammasome formation. It is not cleaved within the FIIND domain, does not assemble into specks, nor promote IL1B release (PubMed:22665479). However, in an vitro cell-free system, it has been shown to be activated by MDP (PubMed:17349957). Binds ATP (PubMed:11113115, PubMed:15212762). [The UniProt Consortium]