Cat: IPD-X33583

Recombinant Pseudomonas cichorii DTE Protein,His & Myc

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Analytical Data

  • Gene name

    DTE

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (DTE)(D-ribulose 3-epimerase)(Ketose 3-epimerase)

  • Species

    Pseudomonas cichorii

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O50580

  • Expression Region

    1-290aa

  • Molecular Weight

    40.1 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

DTE (Dipeptidyl Peptidase IV, also known as DPP-4) is a key enzyme involved in various physiological processes, including glucose metabolism, immune response, and cellular signaling. Its role in the inactivation of several bioactive peptides, such as incretins, has made it a target of significant interest in diabetes research, particularly in the context of type 2 diabetes management. Recent studies have highlighted the importance of DTE's structural and functional characteristics, as they can influence substrate specificity and enzymatic activity. Advances in recombinant DNA technology have enabled the production of modified DTE proteins, allowing researchers to explore their potential therapeutic applications, including as inhibitors in diabetic therapies and modulators of immune responses. The investigation of DTE's role extends beyond diabetes; its implications in cancer biology and cardiovascular health have started to emerge, underscoring the necessity for a deeper understanding of its mechanisms. As the field advances, there is a growing emphasis on structure-function relationships, which could pave the way for novel therapeutic strategies targeting DTE and related pathways, ultimately improving health outcomes in various diseases.

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