Analytical Data
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Gene name
NLRP3
- Application
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Alternative Names
NACHT, LRR and PYD domains-containing protein 3(Angiotensin/vasopressin receptor AII/AVP-like)(Caterpiller protein 1.1)(CLR1.1)(Cold-induced autoinflammatory syndrome 1 protein)(Cryopyrin)(PYRIN-containing APAF1-like protein 1)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96P20
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Expression Region
733-1036aa
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Molecular Weight
40.7 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
NLRP3 (NACHT, LRR and PYD domains-containing protein 3) is a key component of the innate immune system and plays a pivotal role in the formation of the NLRP3 inflammasome, a multiprotein complex that activates caspase-1 and promotes the secretion of pro-inflammatory cytokines such as IL-1β and IL-18. Dysregulation of NLRP3 has been implicated in various inflammatory diseases, including autoinflammatory syndromes, metabolic disorders, and neurodegenerative diseases. Given its critical role in inflammation, NLRP3 has emerged as a promising therapeutic target for treating chronic inflammatory conditions. The study of recombinant NLRP3 protein allows researchers to explore its structural and functional properties, elucidate the mechanisms of inflammasome activation, and identify potential inhibitors. Furthermore, producing recombinant NLRP3 in a controlled laboratory setting facilitates the examination of its interactions with other regulatory proteins and its response to various stimuli. This research is essential for understanding the pathophysiology of diseases associated with NLRP3, paving the way for the development of novel anti-inflammatory therapies that can specifically modulate NLRP3 activity. As our understanding of the inflammasome and its complex regulatory mechanisms expands, recombinant NLRP3 will continue to be a valuable tool in both basic and translational research aimed at mitigating the effects of excessive inflammation in human health.
