Cat: IPD-X40151

Recombinant Treponema pallidum tpd Protein ,His & Myc

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Analytical Data

  • Gene name

    tpd

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Pathogen-specific membrane antigen

  • Species

    Treponema pallidum

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P19478

  • Expression Region

    20-204aa

  • Molecular Weight

    27.1 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

TPD (Tobacco etch virus protease) is a highly efficient protease widely used in recombinant protein expression and purification systems. Research into TPD and its applications has become increasingly significant due to its ability to cleave specifically at the N-terminus of proteins, thereby facilitating the production of properly folded and functional proteins. This specificity is particularly valuable in the biotechnology and pharmaceutical industries, where the need for high-quality recombinant proteins is critical for therapeutic development and research. Unlike traditional proteases, TPD exhibits minimal recognition of native protein sequences, reducing the risk of unintended cleavage and enhancing the yield of desired products. Furthermore, its robust activity across a range of conditions makes TPD an ideal candidate for diverse applications, including the generation of protein tags, peptide synthesis, and the production of complex multiprotein assemblies. The ongoing exploration of TPD's engineering and optimization is paving the way for improved methods in protein production, making it a cornerstone in the field of recombinant protein technology. As researchers continue to unravel the intricacies of TPD's structure and function, its applications are expected to expand, contributing significantly to advancements in biotechnology and molecular biology.

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