Analytical Data
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Gene name
NLRP3
- Application
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Alternative Names
Cold autoinflammatory syndrome 1 protein homolog Cryopyrin Mast cell maturation-associated-inducible protein 1 PYRIN-containing APAF1-like protein 1
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Species
Mouse
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8R4B8
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Expression Region
1-153aa
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Molecular Weight
34.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
The NLRP3 (NOD-like receptor family pyrin domain containing 3) protein plays a crucial role in the innate immune system, acting as a key component of the inflammasome complex that mediates the activation of inflammatory cytokines, particularly interleukin-1β (IL-1β). Dysregulation of NLRP3 has been implicated in various autoinflammatory diseases, such as familial Mediterranean fever, CAPS (Cryopyrin-associated periodic syndromes), and systemic lupus erythematosus, as well as in metabolic disorders like type 2 diabetes and atherosclerosis. Research into NLRP3 recombinant proteins has gained momentum as scientists seek to elucidate its structural and functional properties, which could provide insights into its regulatory mechanisms and potential therapeutic targets. By modifying and expressing NLRP3 in heterologous systems, researchers can study its interactions with other inflammasome components, explore the effects of mutations associated with disease, and assess how environmental triggers can influence its activation. Furthermore, understanding the dynamics of NLRP3 activation and inhibition at the molecular level may pave the way for developing novel anti-inflammatory drugs aimed at controlling aberrant NLRP3 activation in various diseases. Overall, the study of NLRP3 recombinant proteins is pivotal for advancing our understanding of immune responses and for designing targeted therapies for inflammation-related conditions.
