Cat: IPD-X30956

Recombinant Human DPEP1 Protein (Yeast),His

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Analytical Data

  • Gene name

    DPEP1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (Beta-lactamase)(Dehydropeptidase-I)(Microsomal dipeptidase)(Renal dipeptidase)(hRDP)

  • Species

    Human

  • Source

    Yeast

  • Tag

    C- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P16444

  • Expression Region

    17-385aa

  • Molecular Weight

    42.5 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

DPEP1 (Dipeptidase 1), also known as renal dipeptidase or solute carrier family 15 member 1 (SLC15A1), is a membrane-bound enzyme that predominantly expresses in the kidneys and plays a crucial role in the hydrolysis of dipeptides, facilitating amino acid absorption. Research into DPEP1 has gained momentum due to its implications in renal physiology, peptide metabolism, and various pathological conditions, including hypertension, diabetes, and kidney diseases. The enzyme's activity in the proximal tubules of the kidneys contributes to the reclamation of amino acids and the overall maintenance of nitrogen balance in the body. Furthermore, disruptions in DPEP1 function can lead to impaired peptide transport and altered amino acid profiles, potentially exacerbating metabolic disorders. Scientists are particularly interested in DPEP1 as a therapeutic target, exploring its modulation for enhancing amino acid reabsorption and improving nutritional outcomes in patients with renal impairment. Additionally, recombinant DPEP1 protein has become a valuable tool in structural biology and enzymology studies, allowing researchers to investigate its catalytic mechanisms and interactions at a molecular level. Understanding the biochemical and regulatory pathways involving DPEP1 can thus provide insights into its broader physiological roles and therapeutic potential, paving the way for innovative approaches in the management of related diseases.

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