Cat: IPD-X36854

Recombinant Human EPT1 Protein,His

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Analytical Data

  • Gene name

    EPT1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SLC15A1; HPECT1; PEPT1; Solute Carrier Family 15 Member 1,Oligopeptide Transporter; Oligopeptide transporter, small intestine isoform; Intestinal H(+)/peptide cotransporter

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P46059

  • Expression Region

    Asp383~Gln584

  • Molecular Weight

    27kDa

  • 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

EPT1, or endoplasmic reticulum protein 1, is a critically important protein that plays a key role in the endoplasmic reticulum (ER) functions, particularly in the context of protein folding, maturation, and quality control. Research on EPT1 has gained traction due to its potential implications in various disease states, including neurodegenerative conditions, cancer, and metabolic disorders. Understanding the molecular mechanisms underlying EPT1's function can provide insights into the pathophysiology of these diseases, as well as highlight its potential as a therapeutic target. Recombinant EPT1 protein is produced for various applications, including structural studies, functional assays, and drug screening. Advances in recombinant DNA technology have made it feasible to produce EPT1 in sufficient quantities and with necessary post-translational modifications, enabling researchers to explore its biochemical properties and interactions in greater detail. Additionally, investigations into EPT1's role in ER stress responses and unfolded protein response pathways underscore its significance in cellular homeostasis and signal transduction. As the understanding of EPT1's functions and dynamics in cellular environments expands, it holds promise not only as a biomarker for disease diagnosis but also as a potential agent in therapeutic development, aimed at restoring normal ER function and alleviating disease symptoms.

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