Analytical Data
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Gene name
NLRP2
- Application
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Alternative Names
NALP2; NBS1; PAN1; PYPAF2
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Species
Human
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Source
Baculovirus
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NX02-1
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Expression Region
M1-I1062
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Protein Length
Full Length of Isoform-1
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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
NLRP2 (NOD-like receptor family, pyrin domain containing 2) is an important member of the NLR family of proteins, which play a crucial role in the innate immune response. This protein is primarily involved in the recognition of pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs), thereby initiating inflammatory responses. Research has indicated that NLRP2 is implicated in various biological processes, including embryonic development, cell proliferation, and apoptosis. Its dysfunction has been linked to numerous diseases, including autoimmune disorders and certain cancers. Recent studies have focused on the structural and functional characterization of NLRP2, employing recombinant protein techniques to produce the protein in a laboratory setting. This enables researchers to analyze its interaction with ligands and downstream signaling pathways in a controlled environment. Additionally, understanding the mechanisms by which NLRP2 activates the inflammasome complex is of great significance for developing therapeutic strategies targeting inflammatory diseases. The study of NLRP2 recombinant protein is thus essential for elucidating its role in immune regulation and its potential as a target for novel treatments.
