Analytical Data
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Gene name
eNOS
- Application
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Alternative Names
eNOS；Nostrin
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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
P29474
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Expression Region
61-160aa
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AA Sequence
QPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQ GRPSPGPPAPEQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAAT
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Molecular Weight
37 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
Endothelial nitric oxide synthase (eNOS) is a crucial enzyme responsible for the production of nitric oxide (NO), a signaling molecule that plays a vital role in vascular homeostasis, modulation of blood flow, and regulation of blood pressure. The study of eNOS recombinant protein holds significant importance in cardiovascular research due to its involvement in various pathological conditions, including atherosclerosis, hypertension, and endothelial dysfunction. Understanding the structure and function of eNOS through recombinant technology enables researchers to explore its intricate regulatory mechanisms, post-translational modifications, and interactions with other proteins. By generating eNOS in a controlled laboratory setting, scientists can investigate how alterations in its activity impact vascular health and disease. Furthermore, eNOS recombinant proteins provide valuable tools for developing therapeutic strategies aimed at enhancing NO production or improving eNOS function, which could lead to novel interventions for cardiovascular diseases. Recent advances in molecular biology techniques, such as CRISPR and advanced protein engineering, have also facilitated the generation of eNOS variants with modified characteristics, allowing for deeper explorations of its biological functions. Overall, the research on eNOS recombinant proteins is pivotal in elucidating the role of NO in cardiovascular physiology and pathology, ultimately guiding the development of innovative therapies to combat cardiovascular disorders.
