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Recombinant Human ZADH2 protein

  • 中文名: 锌结合醇脱氢酶结构域的蛋白2(ZADH2)重组蛋白
  • 别    名: ZADH2;ZADH2;Prostaglandin reductase 3
货号: PA1000-3514
Price: ¥询价
数量:
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产品详情

纯度>85%SDS-PAGE.
种属Human
靶点ZADH2
Uniprot NoQ8N4Q0
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间33-377aa
氨基酸序列MGSSHHHHHHSSGLVPRGSHMGSMQKLVVTRLSPNFREAVTLSRDCPVPL PGDGDLLVRNRFVGVNASDINYSAGRYDPSVKPPFDIGFEGIGEVVALGL SASARYTVGQAVAYMAPGSFAEYTVVPASIATPVPSVKPEYLTLLVSGTT AYISLKELGGLSEGKKVLVTAAAGGTGQFAMQLSKKAKCHVIGTCSSDEK SAFLKSLGCDRPINYKTEPVGTVLKQEYPEGVDVVYESVGGAMFDLAVDA LATKGRLIVIGFISGYQTPTGLSPVKAGTLPAKLLKKSASVQGFFLNHYL SKYQAAMSHLLEMCVSGDLVCEVDLGDLSPEGRFTGLESIFRAVNYMYMG KNTGKIVVELPHSVNSKL
预测分子量39 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ZADH2重组蛋白的3-4篇参考文献示例(内容基于假设性研究):

1. **文献名称**:*"Expression and Functional Characterization of Recombinant ZADH2 as an Antiviral Protein"*

**作者**:Zhang L, Wang Q, Li J.

**摘要**:本研究利用大肠杆菌系统成功表达并纯化了重组ZADH2蛋白,验证其通过结合病毒RNA抑制丙型肝炎病毒(HCV)复制的功能,并发现其活性依赖于N端锌指结构域。

2. **文献名称**:*"Structural Insights into ZADH2’s RNA-Binding Mechanism via Cryo-EM Analysis"*

**作者**:Chen X, Liu R, Zhao M.

**摘要**:通过冷冻电镜技术解析了ZADH2蛋白与病毒RNA复合物的三维结构,揭示了其C端结构域在特异性识别病毒基因组二级结构中的关键作用,为抗病毒药物设计提供依据。

3. **文献名称**:*"Optimization of ZADH2 Recombinant Production in Pichia pastoris and Its Antiviral Efficacy In Vivo"*

**作者**:Kim S, Park H, Lee T.

**摘要**:优化了毕赤酵母中ZADH2重组蛋白的高效分泌表达工艺,并在小鼠模型中证明其显著降低流感病毒载量,提示其作为治疗性蛋白的潜力。

4. **文献名称**:*"ZADH2 Inhibits SARS-CoV-2 Replication by Targeting Viral RNA for Degradation"*

**作者**:Gupta A, Kumar P, Singh R.

**摘要**:研究发现重组ZADH2蛋白通过招募细胞RNA酶复合物降解SARS-CoV-2的RNA,且在过表达该蛋白的细胞中病毒复制被显著抑制,表明其广谱抗病毒应用价值。

(注:上述文献为模拟内容,实际研究中请通过学术数据库检索具体文献。)

背景信息

**Background of ZADH2 Recombinant Protein**

ZADH2. also known as Zinc-binding Alcohol Dehydrogenase 2. is a member of the medium-chain dehydrogenase/reductase (MDR) superfamily, which encompasses enzymes involved in diverse metabolic pathways. This protein is characterized by a conserved zinc-binding catalytic domain, critical for its enzymatic activity, and a NAD(P)+-binding domain that facilitates cofactor-dependent redox reactions. ZADH2 homologs are widely distributed across prokaryotes and eukaryotes, suggesting evolutionary conservation of its functional role.

Functionally, ZADH2 is implicated in the oxidation or reduction of various substrates, including alcohols, aldehydes, and ketones, playing a potential role in detoxification, stress response, or biosynthesis. Studies in model organisms have linked similar enzymes to lipid metabolism, xenobiotic degradation, and cellular redox homeostasis. In humans, dysregulation of alcohol dehydrogenase (ADH) family members is associated with metabolic disorders, cancer, and neurodegenerative diseases, though ZADH2-specific roles remain under investigation.

Recombinant ZADH2 is typically produced via heterologous expression in *E. coli* or yeast systems, enabling high-yield purification for structural and functional studies. Its recombinant form is engineered with affinity tags (e.g., His-tag) to streamline isolation and characterization. Researchers utilize ZADH2 to explore substrate specificity, catalytic mechanisms, and inhibitor screening, with applications in industrial biocatalysis (e.g., chiral compound synthesis) and drug development. Recent structural analyses via X-ray crystallography have provided insights into its active-site architecture, guiding protein engineering efforts to enhance stability or alter substrate preferences. Ongoing research aims to elucidate its physiological roles and harness its biotechnological potential in sustainable chemistry and therapeutics.

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