Cat: IPD-X23766

Recombinant Human Collectin-11/CL-K1 Protein (HEK293),His & Myc

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Analytical Data

  • Gene name

    Collectin-11/CL-K1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Collectin kidney protein 1 Short name:CL-K1

  • Species

    Human

  • Source

    HEK293

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BWP8

  • Expression Region

    26-271aa

  • Molecular Weight

    30.1 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

Collectin-11 (CL-K1) is a member of the collectin family of proteins, which play crucial roles in the innate immune response by recognizing a wide range of pathogens. As a collagenous lectin, CL-K1 binds specifically to carbohydrate structures on microbial surfaces, facilitating opsonization and clearance of pathogens. Recent studies highlight its importance in various physiological and pathological conditions, including inflammatory responses, autoimmune diseases, and even cancer progression. Research on CL-K1 has gained momentum due to its potential as a biomarker for disease states and as a therapeutic target. Understanding the structure, function, and interactions of CL-K1 at the molecular level is essential for elucidating its role in immune modulation. Given its unique properties, recombinant CL-K1 protein is being developed for various applications, including vaccine development and as a diagnostic tool. Investigating the mechanisms by which CL-K1 influences immune responses could open new avenues for therapeutic interventions and enhance our comprehension of the immune system's complexities.

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