Cat: IPD-X41036

Recombinant Escherichia coli tsr Protein (Yeast),His

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Analytical Data

  • Gene name

    tsr

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Serine chemoreceptor protein

  • Species

    Escherichia coli

  • Source

    Yeast

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P02942

  • Expression Region

    211-551aa

  • Molecular Weight

    38 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

TSR (TSR1 and TSR2) recombinant proteins have emerged as pivotal targets in the study of ribosome biogenesis and associated cellular processes. These proteins play a critical role in the assembly and maturation of ribosomal RNA and proteins, which are essential for protein synthesis in all living organisms. Research has shown that TSR proteins are involved in the regulation of ribosome function, influencing both translational fidelity and cellular response to stress. As such, understanding TSR protein interactions and their mechanisms can provide valuable insights into the pathogenesis of various diseases, particularly those related to protein synthesis dysfunction, like cancer and genetic disorders. The study of TSR recombinant proteins has gained momentum due to advancements in molecular biology techniques, such as recombinant DNA technology and purification methods, enabling researchers to analyze their structure-function relationships in detail. Furthermore, TSR proteins are also being explored as potential biomarkers and therapeutic targets, highlighting their significance in translational medicine. Overall, ongoing research into TSR recombinant proteins is expected to yield important findings that can contribute to our understanding of fundamental biological processes and enhance the development of novel therapeutic strategies.

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