Cat: IPD-X29754

Recombinant Human Transferrin Protein (HEK293),Avi & His

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Analytical Data

  • Gene name

    Transferrin

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Serotransferrin; Transferrin; Beta-1 metal-binding globulin; Siderophilin; TF; TRF

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-Avi;C-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    AAA61140.1

  • Expression Region

    V20-P698

  • Molecular Weight

    70-85 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

Transferrin is a crucial glycoprotein involved in iron transport within the bloodstream, playing a vital role in cellular iron homeostasis and overall metabolism. It binds iron ions with high affinity, regulating their availability for essential biological processes. The study of recombinant transferrin has gained significance due to its potential therapeutic applications, particularly in iron deficiency disorders and conditions requiring controlled iron delivery. Recombinant technology allows for the production of transferrin in a laboratory setting, enabling the creation of variants or engineered forms with enhanced properties, such as improved binding affinity or altered release profiles. Such advancements may lead to innovative treatments for diseases associated with abnormal iron metabolism, including anemia, hemochromatosis, and certain cancers. Furthermore, recombinant transferrin can be utilized in drug delivery systems, facilitating the targeted transport of therapeutic agents into specific cells or tissues, particularly cancer cells that often overexpress transferrin receptors. The ongoing research into transferrin and its recombinant forms not only enhances our understanding of iron biology but also opens new avenues for the development of effective and safer therapeutic strategies.

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