protein

NLRP1 Protein, Human

HY-P702188

10 μg

270 USD

NLRP1 Protein, Human

proteins

E. coli

10 μg

270 USD

The NLRP1 protein is a key sensor in the NLRP1 inflammasome and can trigger pyroptosis in response to multiple pathogen-related signals. It acts as a pattern recognition receptor (PRR), recognizes pathogens and damage-related signals, and initiates inflammasome complex formation and CASP1 activation. NLRP1 Protein, Human is the recombinant human-derived NLRP1 protein, expressed by E. coli , with tag free. The total length of NLRP1 Protein, Human is 84 a.a., .

Human

The NLRP1 protein serves as the pivotal sensor component within the NLRP1 inflammasome, orchestrating inflammasome activation in response to diverse pathogen-associated signals. This activation culminates in pyroptosis, a critical cellular defense mechanism. Inflammasomes, supramolecular complexes that assemble in the cytosol, play indispensable roles in innate immunity and inflammation. Functioning as a recognition receptor (PRR), NLRP1 discerns specific pathogens and damage-associated signals, including cleavage by certain human enteroviruses, double-stranded RNA, UV-B irradiation, and Val-boroPro inhibitor. Upon detection, NLRP1 initiates the formation of the inflammasome polymeric complex, consisting of NLRP1, CASP1, and PYCARD/ASC. In response to pathogen-associated cues, the N-terminal portion of NLRP1 undergoes proteasomal degradation, liberating the cleaved C-terminal segment. This C-terminal fragment polymerizes and associates with PYCARD/ASC, instigating the inflammasome complex formation. The NLRP1 inflammasome recruits pro-caspase-1, fostering CASP1 activation, subsequently cleaving and activating inflammatory cytokines IL1B and IL18, along with gasdermin-D (GSDMD), ultimately inducing pyroptosis. In the absence of GSDMD expression, the NLRP1 inflammasome recruits and activates CASP8, leading to the activation of gasdermin-E (GSDME). Activation of the NLRP1 inflammasome is also crucial for HMGB1 secretion, amplifying inflammatory responses. NLRP1 additionally binds ATP, displaying ATPase activity, playing a pivotal role in antiviral immunity and inflammation in the human airway epithelium. It recognizes various pathogen-associated signals, such as HRV-14 and HRV-16 infection, positive-strand RNA viruses, and long dsRNA, acting as a direct sensor for RNA virus infection. Furthermore, NLRP1 may be activated by muramyl dipeptide (MDP) in a NOD2-dependent manner. UV-B irradiation causing ribosome collisions activates the NLRP1 inflammasome, and it functions as the precursor of the inflammasome, mediating autoproteolytic processing within the FIIND domain to generate N-terminal and C-terminal segments, which associate non-covalently in the absence of pathogens and other damage-associated signals.

NLRP1; NACHT; LRR and PYD domains-containing protein 1; Caspase recruitment domain-containing protein 7; Death effector filament-forming ced-4-like apoptosis protein; Nucleotide-binding domain and caspase recruitment domain

Greater than 90% as determined by reducing SDS-PAGE.

Supplied as a 0.22 μm filtered solution of 50 mM Tris-HCl, pH7.5, 200 mM NaCl, 20% glycerol.

Shipping with dry ice