Cat: IPD-X38210

Recombinant Mouse TCN2 Protein(HEK293),His

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Analytical Data

  • Gene name

    TCN2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    TC2; Transcobalamin II

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O88968

  • Expression Region

    Glu19~Trp430

  • Molecular Weight

    46kDa

  • 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

TCN2, or Transcobalamin II, is a key protein involved in the intracellular transport of vitamin B12, an essential nutrient for DNA synthesis, neurological function, and red blood cell formation. Deficiencies in TCN2 can lead to impaired vitamin B12 transport, resulting in megaloblastic anemia and neurological disorders. Research on TCN2 recombinant protein has gained traction due to its potential therapeutic implications in treating vitamin B12-related deficiencies and understanding its role in cellular metabolism. The protein's structure and function have been extensively studied to elucidate its binding mechanisms with vitamin B12 and its subsequent delivery to target cells. Advances in biotechnology have enabled the production of TCN2 as a recombinant protein, facilitating high-yield purification and functional studies. Investigating TCN2's interaction with various cellular receptors and its influence on vitamin B12 metabolism could provide insights into metabolic disorders and lead to novel therapeutic strategies. Additionally, exploring TCN2 variations and their associations with genetic disorders highlights its significance in personalized medicine. As research progresses, TCN2 recombinant protein continues to be a promising focal point for developing diagnostic tools and therapeutic agents targeting vitamin B12 deficiency and related health issues.

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