Analytical Data
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基因名
NOXO1
- Application
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别名
NADPH oxidase organizer 1; NADPH oxidase regulatory protein; Nox organizer 1; Nox organizing protein 1; Nox-organizing protein 1; NOXO1; NOXO1_HUMAN; P41NOX; Regulatory protein P41NOX; SH3 and PX domain-containing protein 5; SH3PXD5
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8NFA2
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表达区间
1-376 aa
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氨基酸序列
MAGPRYPVSV QGAALVQIKR LQTFAFSVRW SDGSDTFVRR SWDEFRQLKK TLKETFPVEA GLLRRSDRVL PKLLGQASLD APLLGRVGRT SRGLARLQLL ETYSRRLLAT AERVARSPTI TGFFAPQPLD LEPALPPGSR VILPTPEEQP LSRAAGRLSI HSLEAQSLRC LQPFCTQDTR DRPFQAQAQE SLDVLLRHPS GWWLVENEDR QTAWFPAPYL EEAAPGQGRE GGPSLGSSGP QFCASRAYES SRADELSVPA GARVRVLETS DRGWWLCRYG DRAGLLPAVL LRPEGLGALL SGTGFRGGDD PAGEARGFPE PSQATAPPPT VPTRPSPGAI QSRCCTVTRR ALERRPRRQG RPRGCVDSVP HPTTEQ
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分子量
41.2 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
NOXO1 (NADPH oxidase organizer 1) is a crucial component of the NADPH oxidase enzyme complex, which plays a significant role in regulating reactive oxygen species (ROS) generation in various cell types. These ROS are important for cellular signaling, host defense, and inflammation but can also contribute to oxidative stress and various diseases when dysregulated. Due to NOXO1's pivotal role in NADPH oxidase activation and its implication in pathophysiological processes such as cardiovascular diseases, cancer, and neurodegenerative disorders, understanding its structural and functional characteristics is essential. Recombinant NOXO1 protein studies allow researchers to explore its interaction with other NADPH oxidase components and to elucidate its regulatory mechanisms. This research not only provides insights into the fundamental biology of ROS production and signaling pathways but also opens avenues for potential therapeutic interventions targeting NOXO1 in disease contexts. By employing recombinant protein technology, scientists can produce large quantities of pure NOXO1, facilitating biochemical and biophysical analyses, as well as high-throughput screening for inhibitors or modulators. Overall, the study of NOXO1 recombinant protein is vital for advancing our understanding of redox biology and for developing novel therapeutic strategies aimed at mitigating the detrimental effects of excessive ROS in diverse diseases.
