Anti-NLRP1 antibody (STJA0007059)

SKU:
STJA0007059

Current Stock:
Host: Rabbit
Applications: WB
Reactivity: Human
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-NACHT, LRR and PYD domains-containing protein 1 is suitable for use in Western Blot research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: Liquid in PBS containing 50% Glycerol, 0.5% BSA and 0.02% Sodium Azide.
Purification: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Concentration: 1 mg/mL
Dilution Range: WB 1:500-2000
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: NLRP1
Gene ID: 22861
Uniprot ID: NLRP1_HUMAN
Specificity: This antibody detects endogenous levels of NLRP1 at Human
Immunogen: Synthesized peptide derived from human NLRP1
Post Translational Modifications NACHT, LRR and PYD domains-containing protein 1: Autocatalytically cleaved. Autocatalytic cleavage in FIIND region occurs constitutively, prior to activation signals, and is required for inflammasome activity (IL1B release), possibly by facilitating CASP1 binding. Both N- and C-terminal parts remain associated non-covalently. NACHT, LRR and PYD domains-containing protein 1, N-terminus: Ubiquitinated by the cullin:ZER1/ZYG11B complex in response to pathogen-associated signals, leading to its degradation by the proteasome and subsequent release of the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and forms the NLRP1 inflammasome. Phosphorylated by MAP3K20 isoform ZAKalpha, MAPK11 and MAPK14 in response to UV-B irradiation and ribosome collisions, promoting activation of the NLRP1 inflammasome and pyroptosis. (Microbial infection) Cleaved between Gln-130 and Gly-131 by the Protease 3C from various human enteroviruses and rhinoviruses (EV68, EV71, Coxsackievirus B3, HRV-14 and HRV-16). This cleavage triggers N-glycine-mediated proteasomal degradation of the autoinhibitory NLRP1 N-terminal fragment via the cullin:ZER1/ZYG11B complex which liberates the activating C-terminal fragment and activates NLRP1 inflammasome. (Microbial infection) Cleaved between Gln-333 and Gly-334 by the 3C-like proteinase nsp5 from human coronavirus SARS-CoV-2. This cleavage liberates the activating C-terminal fragment and activates NLRP1 inflammasome, leading to downstream activation of GSDME and lung epithelial cell death.
Function Acts as the sensor component of the NLRP1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as cleavage by some human enteroviruses and rhinoviruses, double-stranded RNA, UV-B irradiation, or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex composed of NLRP1, CASP1 and PYCARD/ASC. In response to pathogen-associated signals, the N-terminal part of NLRP1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and associates with PYCARD/ASC to initiate the formation of the inflammasome complex: the NLRP1 inflammasome recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis. In the absence of GSDMD expression, the NLRP1 inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME). Activation of NLRP1 inflammasome is also required for HMGB1 secretion.the active cytokines and HMGB1 stimulate inflammatory responses. Binds ATP and shows ATPase activity. Plays an important role in antiviral immunity and inflammation in the human airway epithelium. Specifically recognizes a number of pathogen-associated signals: upon infection by human rhinoviruses 14 and 16 (HRV-14 and HRV-16), NLRP1 is cleaved and activated which triggers NLRP1-dependent inflammasome activation and IL18 secretion. Positive-strand RNA viruses, such as Semliki forest virus and long dsRNA activate the NLRP1 inflammasome, triggering IL1B release in a NLRP1-dependent fashion. Acts as a direct sensor for long dsRNA and thus RNA virus infection. May also be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner. The NLRP1 inflammasome is also activated in response to UV-B irradiation causing ribosome collisions: ribosome collisions cause phosphorylation and activation of NLRP1 in a MAP3K20-dependent manner, leading to pyroptosis. NACHT, LRR and PYD domains-containing protein 1: Constitutes the precursor of the NLRP1 inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. NACHT, LRR and PYD domains-containing protein 1, N-terminus: Regulatory part that prevents formation of the NLRP1 inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of NLRP1 (NACHT, LRR and PYD domains-containing protein 1, C-terminus), preventing activation of the NLRP1 inflammasome. In response to pathogen-associated signals, this part is ubiquitinated and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the NLRP1 inflammasome. NACHT, LRR and PYD domains-containing protein 1, C-terminus: Constitutes the active part of the NLRP1 inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of NLRP1 (NACHT, LRR and PYD domains-containing protein 1, N-terminus), preventing activation of the NLRP1 inflammasome. In response to pathogen-associated signals, the N-terminal part of NLRP1 is degraded by the proteasome, releasing this form, which polymerizes and associates with PYCARD/ASC to form of the NLRP1 inflammasome complex: the NLRP1 inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis. Isoform 2: It is unclear whether is involved in inflammasome formation. It is not cleaved within the FIIND domain, does not assemble into specks, nor promote IL1B release. However, in an vitro cell-free system, it has been shown to be activated by MDP.
Protein Name 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 Cleaved Into - Nacht - Lrr And Pyd Domains-Containing Protein 1 - C-Terminus
Nlrp1-Ct - Nacht - Lrr And Pyd Domains-Containing Protein 1 - N-Terminus
Nlrp1-Nt
Database Links Reactome: R-HSA-844455
Cellular Localisation Cytoplasm
Cytosol
Nucleus
Nucleocytoplasmic Distribution In Lymphoid Organs (Probably In T-Cells) And In Neurons
In Epithelial Cells
Predominantly Cytoplasmic
Nacht
Lrr And Pyd Domains-Containing Protein 1
C-Terminus: Inflammasome
N-Terminus: Nucleus
(Microbial Infection) Interaction With Human Herpes Virus 8/Hhv-8 Proteins Orf45 Promotes Translocation Of The N-Terminal Part Of Nlrp1 Into The Nucleus
Relieving Autoinhibition Of The Nlrp1 Inflammasome And Leading To Its Activation
Alternative Antibody Names Anti-Nacht - Lrr And Pyd Domains-Containing Protein 1 antibody
Anti-Caspase Recruitment Domain-Containing Protein 7 antibody
Anti-Death Effector Filament-Forming Ced-4-Like Apoptosis Protein antibody
Anti-Nucleotide-Binding Domain And Caspase Recruitment Domain Cleaved Into - Nacht - Lrr And Pyd Domains-Containing Protein 1 - C-Terminus antibody
Anti-Nlrp1-Ct - Nacht - Lrr And Pyd Domains-Containing Protein 1 - N-Terminus antibody
Anti-Nlrp1-Nt antibody
Anti-NLRP1 antibody
Anti-CARD7 antibody
Anti-DEFCAP antibody
Anti-KIAA0926 antibody
Anti-NAC antibody
Anti-NALP1 antibody

Information sourced from Uniprot.org

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