Analytical Data
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基因名
Nos3
- Application
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别名
Constitutive NOS ;cNOSEC-NOSEndothelial NOS ;eNOSNOS type III ;NOSIII
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种属
Rat
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q62600
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表达区间
519-690aa
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分子量
22.9 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.












