NLRP6 Protein, Human (Sf9)

The NLRP6 protein serves as the central sensor of the NLRP6 inflammasome, driving inflammasome activation in response to various pathogen-related signals. It recognizes specific pathogen- and damage-associated signals, such as lipoteichoic acid (LTA) and double-stranded RNA (dsRNA), initiating liquid-liquid phase separation (LLPS) to form complexes. NLRP6 Protein, Human (Sf9) is the recombinant human-derived NLRP6 protein, expressed by Sf9 insect cells , with tag free. The total length of NLRP6 Protein, Human (Sf9) is 892 a.a., .

The NLRP6 protein functions as the key sensor component within the NLRP6 inflammasome, orchestrating inflammasome activation in response to a spectrum of pathogen-associated signals, ultimately culminating in the maturation and secretion of IL1B and IL18. Inflammasomes, intricate supramolecular complexes assembled in the cytosol in response to pathogens and damage-associated signals, play pivotal roles in innate immunity and inflammation. Operating as a recognition receptor (PRR), NLRP6 discerns and binds specific pathogens and damage-associated signals, such as lipoteichoic acid (LTA) from Gram-positive bacteria, or double-stranded RNA (dsRNA). Although it may also recognize lipopolysaccharide (LPS), a major component of Gram-negative bacteria, it is likely not a primary activator of the NLRP6 inflammasome. Upon binding LTA or dsRNA, NLRP6 undergoes liquid-liquid phase separation (LLPS), intensifying multivalent interactions, a crucial step for forming the NLRP6 inflammasome polymeric complex. This complex, comprised of NLRP6, PYCARD/ASC, and effector pro-inflammatory caspases (CASP1 and/or CASP4), facilitates the maturation and secretion of IL1B and IL18. The NLRP6 inflammasome assumes a central role in maintaining epithelial integrity and defending against microbial infections in the intestine. It is essential for restricting Gram-positive bacterial infections, recognizing LTA, and recruiting CASP4 and CASP1 for subsequent cytokine maturation and secretion. Additionally, it participates in intestinal antiviral innate immunity, recognizing viral dsRNA, and collaborates with DHX15 to restrict enteric viral infections. Beyond microbial defense, NLRP6 also regulates gut microbiota composition, influences gut mucosal self-renewal and proliferation, and modulates mucus secretion to prevent bacterial invasion. During systemic bacterial infections, the NLRP6 inflammasome negatively regulates neutrophil recruitment and neutrophil extracellular trap (NET) formation. Furthermore, it may contribute to peripheral nerve recovery following injury through an inflammasome-independent mechanism. The NLRP6 inflammasome forms a homomultimeric complex in response to pathogens and damage-associated signals, featuring NLRP6 as the signal sensor, PYCARD/ASC as the adapter, and effector pro-inflammatory caspases (CASP1 and CASP4). The interaction of NLRP6 with PYCARD/ASC, facilitated by liquid-liquid phase separation, initiates nucleation and prion-like polymerization, culminating in CASP1 filament formation and subsequent cytokine release, driving the inflammatory response. Additionally, NLRP6 interacts with DHX15, further expanding its functional repertoire in intestinal antiviral immunity.

Human

Sf9 insect cells

Tag Free

P59044 (M1-F892)

171389

Greater than 80% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.