Analytical Data
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Gene name
EDNRA
- Application
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Alternative Names
Endothelin A receptor ;ET-A ;ETA-R ;hET-AR
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Species
Human
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P25101
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Expression Region
21-80aa
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Molecular Weight
8.8 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
EDNRA, or endothelin receptor type A, is a G protein-coupled receptor that plays a crucial role in various physiological processes, including vascular tone regulation and cell proliferation. Dysregulation of EDNRA signaling has been implicated in several cardiovascular diseases, such as hypertension, heart failure, and pulmonary arterial hypertension. Given its significance in these pathologies, there has been growing interest in the recombinant production of EDNRA to study its structure, function, and potential as a therapeutic target. The development of recombinant EDNRA proteins allows for detailed biochemical assays and crystal structure analysis, which are essential for understanding receptor activation mechanisms and ligand interactions. These studies can also facilitate the identification of novel small molecule inhibitors or modulators, potentially leading to innovative treatments for EDNRA-related diseases. Furthermore, the use of recombinant proteins in cellular assays helps elucidate the downstream signaling pathways activated by EDNRA, enhancing our understanding of how alterations in this receptor contribute to disease states. Collectively, research on recombinant EDNRA not only advances our fundamental knowledge of endothelin receptor biology but also holds promise for clinical applications aimed at addressing various cardiovascular conditions.
