Analytical Data
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Gene name
Cathepsin D
- Application
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Alternative Names
rMuCathepsin D, His; Cathepsin D; CTSD; CPSD
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Species
Mouse
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Source
HEK293
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Tag
C-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P18242
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Expression Region
I21-L410
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AA Sequence
IIRIPLRKFTSIRRTMTEVGGSVEDLILKGPITKYSMQSSPKTTEPVSELLKNYLDAQYYGDIGIGTPPQCFTVVFDTGSSNLWVPSIHCKILDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDQSKARGIKVEKQIFGEATKQPGIVFVAAKFDGILGMGYPHISVNNVLPVFDNLMQQKLVDKNIFSFYLNRDPEGQPGGELMLGGTDSKYYHGELSYLNVTRKAYWQVHMDQLEVGNELTLCKGGCEAIVDTGTSLLVGPVEEVKELQKAIGAVPLIQGEYMIPCEKVSSLPTVYLKLGGKNYELHPDKYILKVSQGGKTICLSGFMGMDIPPPSGPLWILGDVFIGSYYTVFDRDNNRVGFANAVVLHHHHHH
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Protein Length
Full Length of Mature Protein
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Molecular Weight
46 kDa
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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 D is a lysosomal aspartic protease that plays a crucial role in various biological processes, including protein degradation, antigen presentation, and cellular homeostasis. Its dysfunction has been linked to several diseases, such as Alzheimer's disease, cancer, and cardiovascular disorders. The study of recombinant Cathepsin D is essential to understanding its structure-function relationship and biological activity, as it allows for the production of a pure and active form of the enzyme. This enables researchers to investigate its enzymatic properties, substrate specificity, and potential as a therapeutic target. Furthermore, recombinant Cathepsin D can serve as an important tool in drug development pipelines, as well as in the design of specific inhibitors or modulators that could mitigate diseases associated with its dysregulation. The advancement of recombinant DNA technology and expression systems has significantly facilitated the production of this protease, enabling comprehensive studies into its role in health and disease. Through these investigations, a better understanding of Cathepsin D's mechanisms could lead to novel approaches in treating conditions where its activity is altered, highlighting its significance in biomedical research.
