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Recombinant Human ADH3 protein

  • 中文名: 乙醇脱氢酶3(ADH3)重组蛋白
  • 别    名: ADH3;ADH3;Alcohol dehydrogenase 1C
货号: PA2000-1371
Price: ¥询价
数量:
大包装询价

产品详情

纯度>90%SDS-PAGE.
种属Human
靶点ADH3
Uniprot No P00326
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-375aa
氨基酸序列MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNPRGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGFDLLRSGKSIRTVLTF
预测分子量66.7 kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是关于ADH3重组蛋白的模拟参考文献示例(注:内容为示例,非真实文献):

1. **《Heterologous Expression and Characterization of Recombinant Human ADH3》**

- 作者:Smith J, et al.

- 摘要:研究报道了人源ADH3基因在大肠杆菌中的重组表达与纯化,分析了其酶动力学特性,证实其对乙醇和亚硝基化谷胱甘肽(GSNO)的催化活性,为后续功能研究提供基础。

2. **《Structural Insights into ADH3 Catalytic Mechanism by X-ray Crystallography》**

- 作者:Lee H, et al.

- 摘要:通过X射线晶体学解析了重组ADH3的三维结构,揭示了其底物结合口袋的构象变化及锌离子辅因子的作用机制,为靶向药物设计提供结构基础。

3. **《Role of Recombinant ADH3 in Nitric Oxide Signaling and Cellular Redox Regulation》**

- 作者:Wang Y, et al.

- 摘要:利用重组ADH3蛋白探究其在细胞氧化还原平衡中的作用,发现其通过降解S-亚硝基硫醇调控一氧化氮信号通路,影响炎症反应和代谢疾病进程。

4. **《ADH3 as a Potential Drug Target: Inhibitor Screening Using Recombinant Protein》**

- 作者:Garcia R, et al.

- 摘要:基于重组ADH3的高通量抑制剂筛选,发现小分子化合物可特异性抑制其酶活,为酒精依赖或癌症治疗的靶向策略提供实验依据。

(注:以上文献信息为学术示例,实际引用请通过数据库核实真实文献。)

背景信息

**Background of ADH3 Recombinant Protein**

Alcohol dehydrogenase 3 (ADH3), also known as glutathione-dependent formaldehyde dehydrogenase, is a member of the alcohol dehydrogenase (ADH) enzyme family. This class III ADH is evolutionarily conserved and plays a critical role in cellular detoxification and metabolic pathways. Unlike other ADH isoforms primarily involved in ethanol metabolism, ADH3 exhibits a distinct substrate preference for formaldehyde and other small alcohols. It catalyzes the oxidation of formaldehyde to formate, coupled with the reduction of glutathione (GSH) to its oxidized form (GSSG), thereby mitigating the toxicity of endogenous and exogenous aldehydes.

ADH3 is ubiquitously expressed in human tissues, including the liver, brain, and lungs, highlighting its importance in maintaining cellular homeostasis. Its dual functionality—acting both as a formaldehyde dehydrogenase and a nitrosoglutathione reductase—links it to nitric oxide metabolism and oxidative stress regulation. This enzyme also participates in one-carbon metabolism, influencing processes like DNA synthesis and methylation.

Recombinant ADH3 protein is produced using biotechnological platforms, such as *E. coli* or yeast expression systems, enabling large-scale purification for research and industrial applications. Its recombinant form retains the catalytic properties of native ADH3. making it valuable for studying enzyme kinetics, substrate specificity, and inhibitor interactions. Additionally, it serves as a tool in toxicology research to assess aldehyde-related damage and develop therapeutic strategies for conditions linked to oxidative stress or formaldehyde exposure.

The study of recombinant ADH3 has implications for understanding metabolic disorders, cancer (where formaldehyde accumulation may occur), and neurodegenerative diseases. Its role in nitric oxide signaling further suggests potential applications in cardiovascular research. Overall, ADH3 recombinant protein bridges fundamental biochemistry with translational medicine, offering insights into cellular resilience against toxic intermediates.

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