Recombinant Human Nacht, Lrr And Pyd Domains-Containing Protein 1 (NLRP1) Protein (GST)
Beta LifeScience
SKU/CAT #: BLC-01035P
Greater than 85% as determined by SDS-PAGE.
Recombinant Human Nacht, Lrr And Pyd Domains-Containing Protein 1 (NLRP1) Protein (GST)
Beta LifeScience
SKU/CAT #: BLC-01035P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
| Description | Recombinant Human Nacht, Lrr And Pyd Domains-Containing Protein 1 (NLRP1) Protein (GST) is produced by our E.coli expression system. This is a protein fragment. |
| Purity | Greater than 85% as determined by SDS-PAGE. |
| Uniprotkb | Q9C000 |
| Target Symbol | NLRP1 |
| Synonyms | (Caspase recruitment domain-containing protein 7)(Death effector filament-forming ced-4-like apoptosis protein)(Nucleotide-binding domain and caspase recruitment domain) |
| Species | Homo sapiens (Human) |
| Expression System | E.coli |
| Tag | N-GST |
| Target Protein Sequence | MPLDPYHSVTWGHAQGSHHFVFGELRVRPILESLRDEPDPDPRPSREGPAGRVGALARGGPEPCDAASPPGGASCAPELARPREDKSAQQAKLEGGTRLCCRCPEESRLVPGGAVSPGDHVLEVSGTRGTCGCRPRRHAGPELAHS |
| Expression Range | 1-146aa |
| Protein Length | Partial |
| Mol. Weight | 42.9 kDa |
| Research Area | Cell Biology |
| Form | Liquid or Lyophilized powder |
| Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
| Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
| Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
| Target 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 human rhinoviruses 14 and 16 (HRV-14 and HRV-16), double-stranded RNA 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. 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.; Constitutes the precusor 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.; 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.; 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.; 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. |
| Subcellular Location | Cytoplasm, cytosol. Cytoplasm. Nucleus.; [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Inflammasome. |
| Protein Families | NLRP family |
| Database References | HGNC: 14374 OMIM: 606579 KEGG: hsa:22861 STRING: 9606.ENSP00000460475 UniGene: PMID: 28634744 |
![SDS-PAGE analysis of Human NDUFV1 (Nadh Dehydrogenase [Ubiquinone] Flavoprotein 1, Mitochondrial) - Recombinant Protein, CAT# BLT-08321P, showing >90% purity under 15% SDS-PAGE (Reduced)](http://www.betalifesci.com/cdn/shop/files/1ihmbkjr21vdmc6j_{width}x.jpg?v=1753363793)
