Analytical Data
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Gene name
ECE-1
- Application
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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 95% as determined by SDS-PAGE.
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Uniprot
P42893
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Expression Region
His214~Ala448
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Molecular Weight
33kDa
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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
ECE-1 (Endothelin-Converting Enzyme-1) is a type of metalloprotease that plays a crucial role in the enzymatic conversion of big endothelin-1 (big ET-1) to its biologically active form, endothelin-1 (ET-1), which is a potent vasoconstrictor involved in various physiological and pathological processes, including cardiovascular regulation, cell proliferation, and sodium reabsorption. Understanding the function and regulation of ECE-1 is vital due to its implications in numerous diseases, including hypertension, heart failure, and cancer. The study of ECE-1 recombinant proteins has gained traction in recent years, as these proteins serve as essential tools for exploring the enzyme's structure-function relationships, substrate specificity, and potential inhibitors. The advances in recombinant DNA technology have enabled the production of ECE-1 in various systems, allowing for detailed biochemical characterization and functional studies. Additionally, as ECE-1 is implicated in the pathogenesis of several disorders, research on its recombinant forms provides insights into potential therapeutic targets and drug discovery avenues. Investigating the properties and mechanisms of ECE-1 through recombined proteins holds promise for enhancing our understanding of endothelin biology and developing novel treatments for endothelin-related diseases.
