Analytical Data
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Gene name
EDN1
- Application
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Alternative Names
EDN1；Endothelin-1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05305
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Expression Region
53-73aa
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AA Sequence
CSCSSLMDKECVYFCHLDIIW
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Molecular Weight
29.5kDa
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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
EDN1 (Endothelin-1) is a potent vasoconstrictor peptide that plays a crucial role in various physiological and pathological processes, including cardiovascular regulation, cellular proliferation, and inflammatory responses. Its significance is underscored by its involvement in numerous diseases such as hypertension, heart failure, and cancer. The research on EDN1 recombinant proteins has gained prominence due to their potential therapeutic applications. By producing EDN1 in a recombinant form, researchers can obtain high yields of this peptide, which allows for detailed studies of its biological effects and interactions. Additionally, the recombinant forms can be utilized in drug development and therapeutic interventions aimed at modulating endothelin signaling pathways. Understanding the structure-function relationship of EDN1 through recombinant technologies aids in the identification of specific inhibitors that can target endothelin receptors, potentially leading to novel treatments for conditions associated with endothelial dysfunction. The ongoing research not only seeks to elucidate the molecular mechanisms governing EDN1 activity but also explores its potential as a biomarker for various diseases, highlighting its importance in both basic and translational biomedical research.
