Cat: IPD-X41630

Recombinant Staphylococcus aureus etb Protein ,His & Myc

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Analytical Data

  • Gene name

    etb

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    (Epidermolytic toxin B)

  • Species

    Staphylococcus aureus

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P09332

  • Expression Region

    32-277aa

  • Molecular Weight

    34.8 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

ETB (endothelin B) receptor is a crucial component in various physiological processes, including vasodilation, cell proliferation, and neural development. The ETB receptor is known for its role in mediating the effects of endothelins, a group of potent vasoconstrictors produced by the vascular endothelium. Disruption in ETB signaling has been implicated in several diseases, such as pulmonary hypertension, cardiovascular disorders, and neurological conditions. Research focusing on the recombinant expression of ETB proteins is vital for understanding their structure and function at a molecular level. By employing recombinant DNA technology, researchers can produce ETB proteins in host systems like bacteria, yeast, or mammalian cells, allowing for detailed analysis of their biochemical properties and interactions. Characterizing these proteins through studies such as binding assays, crystallization, and functional assays provides insights into receptor signaling pathways and potential therapeutic targets. Additionally, the generation of specific ETB receptor antagonists or agonists through recombinant techniques can lead to the development of novel drugs aimed at modulating ETB activity, thus paving the way for innovative treatments for related diseases. Overall, the study of recombinant ETB proteins is crucial for advancing our understanding of endothelin biology and developing therapeutic approaches for endothelin-related pathologies.

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