Cat: PA2000-4451

Recombinant Human TXN Protein,His

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Analytical Data

  • Gene name

    TXN

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    TXN;KIAA1652;TRXR2;Thioredoxin reductase 2. mitochondrial

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P10599

  • Expression Region

    2-105aa

  • AA Sequence

    VKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV

  • Molecular Weight

    38.6 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.

Quality inspection process

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Protein Description

The TXN (thioredoxin) protein family, known for its role in redox regulation, has gained significant attention in biomedical research due to its involvement in various cellular processes, including antioxidant defense, cell proliferation, and apoptosis. Originally identified for its function in disulfide bond formation and reduction, TXN has been linked to numerous diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. The overexpression of TXN in tumors suggests its potential as a therapeutic target and a biomarker for cancer diagnosis and prognosis. Furthermore, recent studies have revealed the importance of TXN in regulating immune responses and inflammation, opening avenues for research in autoimmune diseases and infection-related conditions. The characterization of TXN’s structure and function has advanced through recombinant DNA technology, enabling the production of TXN variants with modified properties for experimental and therapeutic applications. Understanding the intricate mechanisms of TXN and its interactions with other cellular components is crucial for developing novel strategies to manipulate its activity for therapeutic benefit. Thus, research on recombinant TXN proteins not only elucidates fundamental biological processes but also holds promise for innovative treatments across a range of diseases.

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