Cat: IPD-X21701

Recombinant Human IDO-1 Protein, His

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Analytical Data

  • Gene name

    IDO-1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CD107B; INDO; Indoleamine-Pyrrole 2,3 Dioxygenase

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P14902

  • Expression Region

    Ala2~Gly403

  • Molecular Weight

    43kDa

  • 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

IDO-1 (Indoleamine 2,3-dioxygenase 1) is an enzyme involved in the catabolism of tryptophan, an essential amino acid, into kynurenine. It plays a critical role in immune regulation and has garnered significant attention in cancer research, as it is often upregulated in tumors, contributing to immune evasion by suppressing T cell activity and promoting regulatory T cell (Treg) generation. The overexpression of IDO-1 in various tumor types, including melanoma, lung cancer, and breast cancer, has been linked to poor prognosis, indicating its potential as a therapeutic target. The enzyme's activity not only affects tumor microenvironments but also has implications in other pathologies, such as autoimmune diseases, infections, and neurodegenerative disorders. Researchers are investigating IDO-1 inhibitors as part of cancer immunotherapy strategies aimed at reinvigorating T cell responses and improving the effectiveness of existing treatments, such as checkpoint inhibitors. Understanding the molecular mechanisms by which IDO-1 operates, as well as its interactions with other immune modulators, is crucial to developing novel therapeutic approaches. Additionally, IDO-1's role in altering systemic metabolism and influencing the microbiome further emphasizes the complexity of its function in health and disease. Given these factors, IDO-1 represents a promising candidate for targeted therapies, warranting ongoing research to elucidate its full potential in clinical applications.

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