Cat: IPD-X41818

Recombinant Bovine PTER Protein,His & Myc

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Analytical Data

  • Gene name

    PTER

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (Parathion hydrolase-related protein)

  • Species

    Bovine

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A6QLJ8

  • Expression Region

    1-349aa

  • Molecular Weight

    46.5 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.

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Protein Description

The study of PTER (positive regulatory domain-containing protein) recombinant proteins has emerged as a significant area of interest in molecular biology and biotechnology due to its potential implications in understanding cellular processes and disease mechanisms. PTER is involved in various regulatory functions, including gene expression, cell differentiation, and proliferation, making it a critical component in signaling pathways related to cancer and other diseases. Investigating PTER through recombinant protein technology allows for the production of large quantities of the protein, facilitating in-depth functional studies and structural analyses. Such studies are essential for elucidating the role of PTER in cellular mechanisms and its interactions with other proteins. Moreover, the generation of these recombinant proteins provides valuable tools for developing therapeutic strategies targeted at the pathways mediated by PTER. As researchers continue to explore its biological significance, the findings could lead to novel insights into disease treatment and the development of biotechnological applications, such as drug development and gene therapy. The integration of PTER studies in the broader context of proteomics and systems biology further enhances its relevance in modern biological research, emphasizing the importance of understanding protein functions in health and disease.

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