Cat: IPD-X40063

Recombinant Corylus avellana albuminImported Protein ,His & SUMO

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Analytical Data

  • Gene name

    albuminImported

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    /

  • Species

    Corylus avellana

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    D0PWG2

  • Expression Region

    23-147aa

  • Molecular Weight

    30.9 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.

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Protein Description

Albumin is a vital protein in the human body, primarily produced by the liver, and it plays a key role in maintaining oncotic pressure, transporting various substances, and regulating blood volume. Due to its numerous physiological functions, recombinant human albumin (rHA) has garnered significant attention in both research and clinical settings. The production of rHA through recombinant DNA technology offers the advantage of obtaining large quantities of this protein with high purity, addressing limitations associated with traditional extraction methods from human or animal sources, such as the risk of contamination and variability in protein quality. Furthermore, rHA serves as a promising therapeutic candidate in various applications, including drug formulations, as a stabilizer in protein drugs, and as a treatment for conditions like liver failure, burns, and shock. Research on albuminImport, a protein transport system that enhances the intracellular delivery of rHA, aims to improve the efficacy and bioavailability of therapeutic proteins, thereby expanding their clinical utility. Understanding the mechanisms behind albuminImport can lead to advancements in drug delivery systems and personalized medicine, paving the way for innovative therapeutic options. The continued exploration of albumin and its recombinant forms is essential in addressing unmet medical needs and improving patient outcomes across a range of diseases.

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