Cat: IPD-X40335

Recombinant Mouse K Protein ,His & Myc

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Analytical Data

  • Gene name

    K

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Ig kappa chain V-V region K2; Fragment

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P01635

  • Expression Region

    21-115aa

  • Molecular Weight

    17.4 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

K-recombinant proteins, often referred to as K-proteins, represent a crucial area of research in molecular biology and biotechnology due to their diverse applications in medicine, agriculture, and industry. These proteins are typically derived from various organisms, including plants, bacteria, and animals, and are engineered to exhibit specific properties beneficial for therapeutic purposes. The study of K-recombinant proteins has gained momentum with advancements in genetic engineering techniques, such as recombinant DNA technology and CRISPR, which allow for precise modifications at the molecular level. This research is particularly important for the production of biopharmaceuticals, where K-proteins can be designed to act as vaccines, enzymes, or other therapeutic agents. Additionally, K-proteins are pivotal in developing genetically modified crops that possess enhanced traits such as pest resistance or improved nutritional value. The ability to produce large quantities of these proteins efficiently and cost-effectively has significant implications for food security and public health. Overall, the research on K-recombinant proteins not only enhances our understanding of protein function and interaction but also holds the promise of addressing some of the world's most pressing challenges in health and agriculture.

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