Cat: IPD-X41704

Recombinant Human DDTL Protein ,His & Myc

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Analytical Data

  • Gene name

    DDTL

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (D-dopachrome tautomerase-like protein)

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A6NHG4

  • Expression Region

    1-134aa

  • Molecular Weight

    21.6 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

DDTL (Double-Domain Toxin-Like) recombinant proteins have garnered significant attention in the field of biochemistry and molecular biology due to their unique structural and functional properties. Originally inspired by natural toxin proteins, which exhibit potent biological activities, researchers have sought to harness the potential of DDTL proteins for various applications, including therapeutic development and biotechnological innovations. The study of DDTL proteins is driven by their dual-domain architecture, which allows for enhanced specificity and functionality by combining distinct biochemical properties from each domain. This has opened avenues for creating novel biosensors, targeted drug delivery systems, and therapeutic agents with reduced side effects. Additionally, DDTLs' capacity for engineering and modification makes them valuable candidates in the ongoing quest to design more effective and safe biomolecules. Research has focused on elucidating the mechanisms of action of these proteins, optimizing their production in recombinant systems, and exploring their interactions with biological targets. As a result, DDTL proteins represent a promising frontier in the development of advanced materials and therapeutics, with the potential to address various challenges in medicine and biotechnology.

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