Cat: IPD-X41812

Recombinant Larimichthys crocea receptor Protein,His

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Analytical Data

  • Gene name

    receptor

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Larimichthys crocea

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    F2XEX3

  • Expression Region

    1-308aa

  • Molecular Weight

    37.0 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

Receptor recombinant proteins have garnered significant attention in the fields of molecular biology, pharmacology, and drug development due to their pivotal role in mediating cellular responses to a variety of extracellular signals. These proteins, which include various types of receptors such as G protein-coupled receptors (GPCRs), ion channels, and receptor tyrosine kinases, are integral to numerous physiological processes, including cell signaling, growth, and differentiation. The study of recombinant receptors has advanced considerably with the advent of genetic engineering techniques, allowing for the expression of these proteins in host systems like bacteria, yeast, and mammalian cells. This capability is essential for elucidating receptor structure-function relationships, understanding their signaling pathways, and screening potential drug candidates that target these receptors. Additionally, recombinant receptors are crucial for therapeutic applications, such as the development of monoclonal antibodies and small-molecule drugs that modulate receptor activity. As the demand for innovative therapies increases, researching receptor recombinant proteins not only enhances our understanding of fundamental biological processes but also paves the way for the discovery of novel therapeutics aimed at treating various diseases.

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