Cat: IPD-X39973

Recombinant Human RDH11 Protein ,His & SUMO

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Analytical Data

  • Gene name

    RDH11

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Androgen-regulated short-chain dehydrogenase/reductase 1HCV core-binding protein HCBP12;Prostate short-chain dehydrogenase/reductase 1Retinal reductase 1 ;RalR1Short chain dehydrogenase/reductase family 7C member 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8TC12

  • Expression Region

    22-318aa

  • Molecular Weight

    49 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

RDH11, or Retinol Dehydrogenase 11, is a key enzyme involved in the metabolism of retinoids, which are essential for various biological processes including vision, cell differentiation, and embryonic development. The protein plays a critical role in the conversion of retinol (vitamin A) into active retinaldehyde, influencing the availability of retinoids for vital physiological functions. Research into RDH11 has gained traction due to its potential implications in developmental disorders, cancer progression, and other diseases linked to retinoid metabolism. Moreover, understanding the structural and functional properties of RDH11 could pave the way for therapeutic strategies targeting retinoid-related pathways. Recombinant RDH11 protein production allows scientists to study its enzymatic activity, interaction with retinoids, and its regulation under different physiological conditions. By characterizing this protein in vitro and in animal models, researchers aim to elucidate its precise role in health and disease, which may offer new insights for drug development and personalized medicine approaches in treating conditions associated with retinoid dysregulation. Thus, RDH11 not only serves as a vital tool in developmental biology but also holds promise as a target for future therapeutic interventions.

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