Cat: IPD-X30874

Recombinant Human Cathepsin K Protein (Yeast),His

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Analytical Data

  • Gene name

    Cathepsin K

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Cathepsin OCathepsin O2;Cathepsin X

  • Species

    Human

  • Source

    Yeast

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P43235

  • Expression Region

    115-329aa

  • Molecular Weight

    25.5 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

Cathepsin K is a lysosomal cysteine protease primarily expressed in osteoclasts, playing a crucial role in bone resorption and remodeling. It has garnered significant attention in biomedical research due to its implications in various diseases, including osteoporosis, arthritis, and certain forms of cancer. The enzyme's ability to degrade collagen and other extracellular matrix components makes it vital in the pathological processes of bone degradation and tissue remodeling. Researchers have focused on producing recombinant Cathepsin K to facilitate in vitro studies, enabling a better understanding of its enzymatic mechanisms and substrate specificity. The recombinant protein provides a reliable and abundant source for screening potential inhibitors that could serve as therapeutic agents for conditions characterized by excessive bone resorption. Additionally, structural studies of recombinant Cathepsin K have offered insights into its active site and the conformational changes associated with its catalytic activity. This research is critical for developing targeted inhibitors that can effectively modulate Cathepsin K activity, ultimately leading to novel treatment strategies for bone-related disorders and improving patient outcomes. As such, the study of recombinant Cathepsin K not only enhances our understanding of its biological functions but also paves the way for innovative therapeutic interventions in diseases where dysregulation of bone metabolism is a key feature.

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