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Human NLRP1 Recombinant Protein (N-His) (HD973012)

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Overview
Catalog No.HD973012
Description
Recombinant Human NLRP1 Protein, N-His (HD973012) expressed in E. coli. Purity: >90% as determined by SDS-PAGE..
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% as determined by SDS-PAGE.
Expression systemE. coli
AccessionQ9C000
Protein lengthThr1088-Ser1473
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesCARD7, Caspase recruitment domain-containing protein 7, DEFCAP, Death effector filament-forming ced-4-like apoptosis protein, EC:3.4.-.-, EC:3.6.4.-, KIAA0926, NAC, NACHT, LRR and PYD domains-containing protein 1, NACHT, LRR and PYD domains-containing protein 1, C-terminus, NACHT, LRR and PYD domains-containing protein 1, N-terminus, NALP1, NLRP1, NLRP1-CT, NLRP1-NT, Nucleotide-binding domain and caspase recruitment domain
Background

NACHT, LRR and PYD domains-containing protein 1 is a ~165 kDa protein. 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).

1. Martinon, F. et al. (2002) Molecular cell 10, 417-26. PMID: 12191486
2. Faustin, B. et al. (2007) Molecular cell 25, 713-24. PMID: 17349957
3. Finger, JN. et al. (2012) The Journal of biological chemistry 287, 25030-7. PMID: 22665479
4. Zhong, FL. et al. (2016) Cell 167, 187-202.e17. PMID: 27662089
5. Drutman, SB. et al. (2019) Proceedings of the National Academy of Sciences of the United States of America 116, 19055-19063. PMID: 31484767
6. Robinson, KS. et al. (2020) Science (New York, N.Y.) 370. PMID: 33093214
7. Tsu, BV. et al. (2021) eLife 10. PMID: 33410748
8. Huang, M. et al. (2021) Nature 592, 773-777. PMID: 33731929
9. Hollingsworth, LR. et al. (2021) Nature 592, 778-783. PMID: 33731932
10. Robinson, KS. et al. (2022) Science (New York, N.Y.) 377, 328-335. PMID: 35857590
Note For research use only
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