Analytical Data
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Gene name
Nos3
- Application
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Alternative Names
Constitutive NOS ;cNOSEC-NOSEndothelial NOS ;eNOSNOS type III ;NOSIII
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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 90% as determined by SDS-PAGE.
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Uniprot
Q62600
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Expression Region
519-690aa
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Molecular Weight
22.9 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
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Protein Description
NOS3, or endothelial nitric oxide synthase (eNOS), is a critical enzyme responsible for the production of nitric oxide (NO) in endothelial cells, which plays a vital role in vascular homeostasis and function. Research into NOS3 has gained significant attention due to its implications in various cardiovascular diseases, including hypertension, atherosclerosis, and heart failure. Dysregulation of NO production can lead to endothelial dysfunction, a key factor in the pathogenesis of these conditions. Recombination proteins of NOS3 are engineered to study the enzyme's structure-function relationship and to explore the molecular mechanisms underlying its regulation and activity. The production of NOS3 recombinant proteins allows for detailed biochemical analyses, enabling researchers to investigate how different post-translational modifications and interactions with other proteins affect its functionality. These studies not only contribute to understanding the physiological role of NOS3 in maintaining vascular health but also hold potential therapeutic implications. By targeting NOS3 or its pathways, novel treatments could be developed to ameliorate cardiovascular diseases associated with NO deficiency or endothelial dysfunction. As interest in personalized medicine grows, the exploration of NOS3 and its recombinant forms continues to be a relevant and promising area of research, particularly in the context of designing targeted therapies aimed at restoring endothelial function.
