NLRP3 (D4D8T) Rabbit mAb recognizes endogenous levels of total NLRP3 protein.

Hamster

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala306 of mouse NLRP3 protein.

The nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family of proteins is a diverse family of cytoplasmic innate immune receptors. They are characterized by the presence of an amino-terminal effector domain, which is often either a caspase activation and recruitment domain (CARD) or a pyrin domain (PYD), followed by a NACHT domain and carboxy-terminal leucine-rich-repeats (LRR) involved in recognition of pathogen-associated molecular patterns (PAMPs) (1). NLR proteins play a variety of roles during the innate immune response including pathogen sensing, transcriptional activation of proinflammatory cytokines through NF-κB, transcriptional activation of type I interferons through IRFs, and formation of inflammasomes leading to activation of inflammatory caspases (1-7).
NLRP3 is an inflammasome-forming NLR that activates caspase-1 leading to maturation of IL-1β and IL-18 (8). The NLRP3 inflammasome is assembled in response to a wide variety of microbial and endogenous stimuli, and therefore it is unlikely the NLRP3 directly interacts with its activators (8). NLRP3 is expressed at highest levels in dendritic cells, monocytes, and macrophages (9).