Analytical Data
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Gene name
catD
- Application
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Alternative Names
(CAT)
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Species
Clostridioides difficile
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P11504
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Expression Region
1-212aa
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Molecular Weight
32.3 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
CatD, or Cathepsin D, is a lysosomal aspartic protease that plays a crucial role in protein degradation and processing within cells. It is involved in various physiological processes, including autophagy, antigen presentation, and tissue remodeling, making it a significant player in both health and disease. Dysregulation of CatD has been linked to several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. Research on CatD recombinant proteins has gained considerable attention due to their potential applications in therapeutic and diagnostic settings. Recombinant expression techniques enable the production of active CatD for studying its structure-function relationships, enzymatic activity, and interaction with other cellular components. Understanding CatD's specific biological roles can lead to the development of targeted therapies and novel biomarkers for diseases associated with its dysfunction. Furthermore, studying CatD in various models can provide insights into its involvement in disease progression and response to treatment. Overall, the exploration of CatD recombinant proteins holds promise for advancing our knowledge of its biology and translating this knowledge into clinical applications.
