纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ADH4 |
Uniprot No | P08319 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-380aa |
氨基酸序列 | MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTD ATVIDSKFEGLAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCR KCKFCLSPLTNLCGKISNLKSPASDQQLMEDKTSRFTCKGKPVYHFFGTS TFSQYTVVSDINLAKIDDDANLERVCLLGCGFSTGYGAAINNAKVTPGST CAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKALGATDCLNPR DLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGV AAGSKGLTVFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDA LVTHTLPFDKISEAFDLMNQGKSIRTILIF |
预测分子量 | 67 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. |
以下是关于ADH4重组蛋白的模拟参考文献示例(非真实文献,仅供格式参考):
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1. **文献名称**:*Expression and Functional Characterization of Recombinant Human ADH4 in Escherichia coli*
**作者**:Smith A, et al.
**摘要**:本研究成功在大肠杆菌中表达了重组人ADH4蛋白,并通过亲和层析纯化获得高纯度产物。酶动力学分析表明,ADH4对乙醇和视黄醇均具有催化活性,提示其在多种代谢途径中的潜在作用。
2. **文献名称**:*Crystal Structure of Recombinant ADH4 Reveals Substrate Binding Specificity*
**作者**:Johnson B, et al.
**摘要**:通过X射线晶体学解析了重组ADH4的三维结构,发现其活性口袋的疏水性残基对长链醇类底物(如视黄醇)具有更高亲和力,为理解ADH家族的底物选择性提供结构基础。
3. **文献名称**:*Evolutionary Analysis of Primate ADH4 via Recombinant Protein Expression*
**作者**:Chen L, et al.
**摘要**:比较了人类与黑猩猩重组ADH4的酶学性质,发现两者在乙醇代谢效率上存在显著差异,可能与灵长类饮食进化中乙醇暴露的变化相关。
4. **文献名称**:*ADH4 Recombinant Protein as a Biocatalyst in Synthetic Chemistry*
**作者**:Müller S, et al.
**摘要**:评估了重组ADH4在体外催化手性醇合成中的应用,证明其在高浓度底物条件下的稳定性和工业应用潜力。
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**注**:以上内容为模拟生成,实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“ADH4 recombinant protein”获取。
ADH4 (Alcohol Dehydrogenase 4) is a member of the alcohol dehydrogenase (ADH) enzyme family, which plays a central role in metabolizing alcohols, including ethanol, retinol, and other endogenous or exogenous substrates. This class I ADH isoform is primarily expressed in the liver and gastrointestinal tract, where it contributes to the oxidation of ethanol into acetaldehyde, a critical step in alcohol detoxification. ADH4 has garnered particular interest due to its evolutionary significance; studies suggest it underwent adaptive changes in primates, potentially linked to dietary shifts that involved fermented fruits. These adaptations may have enhanced ethanol metabolism efficiency, offering insights into human-alcohol coevolution.
Recombinant ADH4 refers to the protein produced through genetic engineering techniques, typically expressed in microbial systems (e.g., *E. coli* or yeast) or mammalian cell cultures. Its production enables controlled studies of enzymatic properties, substrate specificity, and inhibition mechanisms without interference from other ADH isoforms. Researchers often purify recombinant ADH4 using affinity tags (e.g., His-tag) to ensure high yield and purity for structural analyses (e.g., X-ray crystallography) or functional assays.
Beyond its metabolic role, ADH4 has implications in disease research. Dysregulation of ADH4 activity is associated with alcohol-related disorders, certain cancers, and retinoid metabolism defects. Recombinant ADH4 facilitates drug discovery by serving as a target for inhibitors or as a biocatalyst in synthesizing chiral intermediates for pharmaceuticals. Its study also aids in understanding genetic polymorphisms affecting alcohol tolerance and addiction susceptibility. Overall, ADH4 recombinant protein serves as a vital tool for both basic research and applied biotechnology.
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