Cat: IPD-X14924

Recombinant Human TLR4 Protein , His

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Analytical Data

  • Gene name

    TLR4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    hToll (CD_antigen: CD284)

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 85% as determined by SDS-PAGE.

  • Uniprot

    O00206

  • Expression Region

    27-631aa

  • Molecular Weight

    72.4 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

    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.

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Protein Description

Toll-like receptor 4 (TLR4) plays a crucial role in the innate immune response by recognizing pathogen-associated molecular patterns, particularly lipopolysaccharides (LPS) from gram-negative bacteria. The study of TLR4 recombinant proteins has gained significant attention due to their potential in vaccine development, immunotherapy, and understanding immune system mechanisms. Given that TLR4 signaling is fundamental in mediating inflammatory responses, researchers are keen to explore the receptor's structure and function via recombinant technology. Producing TLR4 as a recombinant protein allows for detailed investigations into its binding interactions, signaling pathways, and downstream effects. It also promotes the development of novel therapeutic strategies to modulate immune responses in various diseases, including sepsis, autoimmune disorders, and cancer. Furthermore, TLR4's involvement in the pathogenesis of metabolic conditions, such as obesity and diabetes, underscores the importance of elucidating its functional properties. Overall, continued research on TLR4 recombinant proteins represents a promising avenue for advancing our understanding of immune regulation and for developing new immunotherapeutic interventions.

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