Analytical Data
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Gene name
Cst3
- Application
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Alternative Names
Cystatin-3
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Species
Mouse
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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
P21460
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Expression Region
21-140aa
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Molecular Weight
20.4 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
Related Products
Protein Description
Cst3, or Cystatin C, is a member of the cystatin superfamily of protease inhibitors, primarily implicated in the regulation of proteolytic enzymes, particularly cathepsins. Its role in various physiological processes, including immune response, tissue remodeling, and cell proliferation, has garnered significant interest within the scientific community. Research has shown that altered levels of Cst3 are associated with several pathological conditions, including neurodegenerative diseases, kidney disorders, and certain types of cancer. Furthermore, Cst3 exhibits neuroprotective properties, suggesting its potential as a therapeutic target in conditions such as Alzheimer's disease. Advances in recombinant protein technology have made it feasible to produce Cst3 in large quantities for further investigation into its biological functions and therapeutic applications. The study of recombinant Cst3 not only aids in elucidating its role in pathophysiology but also facilitates the development of novel diagnostic tools and therapeutic strategies, underscoring its importance in both basic and applied research. The continued exploration of Cst3 and its derivatives holds promise for understanding complex biological systems and developing interventions for diseases where cystatin C dysregulation is a contributing factor.











