Analytical Data
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Gene name
Renin
- Application
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Alternative Names
angiotensinogenase
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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
P08424
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Expression Region
Thr144~Val237
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Molecular Weight
11kDa
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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
Renin, an essential enzyme in the renin-angiotensin system (RAS), plays a pivotal role in regulating blood pressure and fluid balance. It is produced primarily in the kidneys and initiates the conversion of angiotensinogen to angiotensin I, which subsequently influences vasoconstriction and aldosterone secretion. Aberrations in renin activity are associated with various cardiovascular and renal disorders, including hypertension, heart failure, and chronic kidney disease. Given its significance, the study of recombinant renin has gained attention as a means to understand its biochemical properties and functional mechanisms. Recombinant proteins allow for detailed investigations into renin's structure-function relationships and its interactions with other components of the RAS. Moreover, the development of recombinant renin provides opportunities for therapeutic applications, such as the development of novel antihypertensive drugs that target this pathway. Advances in biotechnology have facilitated the production of high-purity recombinant renin, making it possible to perform in-depth studies and assays that were previously challenging due to the difficulty of isolating the native enzyme. As a result, research on recombinant renin not only enhances our understanding of hypertension and related diseases but also paves the way for innovative treatment strategies to manage these conditions effectively.
