Analytical Data
-
Gene name
NLRP1
- Application
-
Alternative Names
(Caspase recruitment domain-containing protein 7)(Death effector filament-forming ced-4-like apoptosis protein)(Nucleotide-binding domain and caspase recruitment domain)
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9C000
-
Expression Region
1-146aa
-
Molecular Weight
42.9 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
NLRP1 is a member of the NOD-like receptor (NLR) family of proteins, which play crucial roles in the immune system by detecting pathogens and initiating inflammatory responses. The study of NLRP1 has gained significant attention due to its involvement in various autoimmune diseases and its role in the regulation of inflammatory pathways. Research has demonstrated that NLRP1 is activated by a wide range of stimuli, including microbial components and environmental factors, leading to the formation of the inflammasome complex. This complex is pivotal for the activation of caspase-1, which subsequently cleaves pro-inflammatory cytokines, such as IL-1β and IL-18, facilitating acute inflammatory responses. Furthermore, NLRP1 has been shown to possess mutations that can contribute to diseases like familial Mediterranean fever and other autoinflammatory disorders. The production of recombinant NLRP1 protein allows researchers to study its structure, function, and interactions in the context of these inflammatory processes. This research aids in understanding the mechanistic pathways involved in immune responses and may lead to the development of novel therapeutic strategies targeting NLRP1-related conditions. Overall, the exploration of NLRP1 recombinant protein serves as a vital tool for elucidating the complexities of innate immunity and its implications in human health and disease.
