Analytical Data
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Gene name
Cathepsin S
- Application
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Alternative Names
CTS-S
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q02765
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Expression Region
Leu113~Ile330
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Molecular Weight
29kDa
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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 S is a lysosomal cysteine protease that plays a crucial role in various physiological and pathological processes, including antigen processing, immune response, and tissue remodeling. Its significant involvement in immune cell activation and participation in diseases such as cancer, autoimmune disorders, and cardiovascular diseases has garnered increasing attention from researchers. The enzyme is expressed in various cell types, including macrophages and dendritic cells, and is known to influence the maturation and function of these immune cells. The study of recombinant Cathepsin S proteins has opened new avenues for understanding its biological functions in greater detail. Through recombinant technology, researchers are able to produce active forms of the enzyme, facilitating studies on its enzymatic properties, substrate specificity, and potential therapeutic applications. Moreover, the characterization of Cathepsin S at the molecular level enhances our knowledge regarding its regulation and interplay with other proteases, particularly in inflammatory contexts. As a target for drug development, understanding the structure and function of this enzyme could lead to novel treatments for diseases where Cathepsin S is implicated. This growing body of research underscores the importance of recombinant proteins in elucidating the roles of specific enzymes in health and disease.
