Cat: IPD-X38214

Recombinant Human HAVCR2 Protein(HEK293),His

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Analytical Data

  • Gene name

    HAVCR2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    KIM-3; TIM3; TIMD3; Tim-3; T-cell membrane protein 3; T-cell immunoglobulin mucin receptor 3; T-cell immunoglobulin and mucin domain-containing protein 3

  • Species

    Human

  • Source

    HEK293

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8TDQ0

  • Expression Region

    Ser22~Gly202

  • Molecular Weight

    40-48kDa

  • 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

HAVCR2, also known as T cell immunoglobulin and mucin domain 3 (TIM-3), is a cell surface protein that plays a crucial role in regulating immune responses, particularly in the context of T cell activation and tolerance. Identified as a marker of exhausted T cells, HAVCR2 is increasingly recognized for its implications in various diseases, including cancer, autoimmune disorders, and viral infections. The protein interacts with several ligands, such as galectin-9, leading to the inhibition of Th1 and cytotoxic T lymphocyte (CTL) functions, ultimately contributing to immune evasion by tumors and chronic pathogens. Given its immunomodulatory effects, HAVCR2 has emerged as a potential target for therapeutic interventions aimed at enhancing anti-tumor immunity or reactivating exhausted T cells. Recent studies have focused on the development of HAVCR2 recombinant proteins for diagnostic and therapeutic applications, exploring their roles as biomarkers for disease progression and responsiveness to treatment. Additionally, the potential of HAVCR2 blockade in combination with other immune checkpoint inhibitors is being investigated to improve clinical outcomes in cancer immunotherapy. As research continues to unveil the multifaceted roles of HAVCR2 in immune regulation, understanding its structure, function, and interactions will be essential for harnessing its potential in clinical applications.

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