NLRP6 Rabbit mAb

NLRP6 (NACHT, LRR, and PYD domains-containing protein 6) is a functionally diverse and important member of the NOD-like receptor (NLR) family, originally known as PYPAF5. Its protein structure consists of three core domains: an N-terminal pyrin domain (PYD), a central nucleotide-binding domain (NACHT), and a C-terminal leucine-rich repeat (LRR) domain responsible for recognizing pathogen signals. NLRP6 primarily functions as a sensor of innate immunity, with high expression in intestinal epithelial cells, and plays a critical role in host defense, maintenance of intestinal microecology, and epithelial integrity. Upon recognizing microbial or metabolic signals, it recruits the adaptor protein ASC through its PYD domain, thereby activating caspase-1 and assembling into the NLRP6 inflammasome. This complex promotes the maturation and secretion of pro-inflammatory cytokines such as IL-1β and IL-18, and can induce pyroptosis. In addition, NLRP6 functions also involve regulating the NF-κB and MAPK signaling pathways, responding to viral RNA to induce interferon production, and even participating in the regulation of renal water-salt balance. Studies have shown that NLRP6 dysfunction is closely associated with various pathological processes, including inflammatory bowel disease, colorectal cancer, and metabolic diseases.