Analytical Data
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Gene name
Cathepsin K
- Application
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Alternative Names
CTS-K; CTS02; CTSO; CTSO1; CTSO2; PKND; PYCD; Pycnodysostosis; Cathepsin O; Cathepsin X
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Species
Rhesus Macaque
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P61277
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Expression Region
Pro116~Met329
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Molecular Weight
28kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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.











