Cat: IPD-X28623

Recombinant Human NLRP4 Protein (Baculovirus),His & MBP

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Analytical Data

  • Gene name

    NLRP4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    NALP4; PAN2; PYPAF4; RNH2

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    Strep;His;MBP

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96MN2-1

  • Expression Region

    M1-I994

  • Protein Length

    Full Length of Isoform-1

  • 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

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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

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Protein Description

NLRP4, a member of the NOD-like receptor (NLR) family, plays a crucial role in the innate immune response, particularly in the recognition of pathogens and the regulation of inflammation. As a cytosolic sensor, NLRP4 is involved in forming inflammasomes, which are multiprotein complexes that activate caspases and lead to the release of pro-inflammatory cytokines. Research has indicated that NLRP4 can detect a variety of microbial products, leading to its activation and subsequent inflammatory responses. aberrations in NLRP4 function have been linked to several diseases, including autoimmune disorders and infections. Given its importance in immune regulation, the study of NLRP4 recombinant proteins is essential for understanding its structure-function relationships and mechanisms of action. Recombinant proteins enable researchers to dissect the molecular pathways involved, assess the role of NLRP4 in immune signaling, and develop potential therapeutic strategies targeting NLRP4-related pathologies. Moreover, the production and characterization of recombinant NLRP4 offer valuable insights for drug design and the development of vaccines aimed at modulating immune responses. Overall, the investigation of NLRP4 recombinant proteins is a promising area of research with significant implications for improving our understanding of immune regulation and developing innovative treatments for inflammatory diseases.

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