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Recombinant E.coli atpG2 protein

  • 中文名: 叶绿体ATP合酶γ链2(atpG2)重组蛋白
  • 别    名: atpG2;ATP synthase gamma chain 2, chloroplastic
货号: PA2000-4698
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产品详情

纯度>90%SDS-PAGE.
种属 E.coli
靶点atpG2
Uniprot No Q6LKZ7
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-291aa
氨基酸序列MANAKEIRTKIASVQNTQKITSAMEMVAASKMRKVQDNMAATRPYAENMRKVISHVASGSLEYKHPYLEEREAKRVAYIIISSDRGLCGGLNSNLFKRALTDMRQWQEKNVEVDLTLIGSKAISFFHRFGNVIAQTSGLGDKPKLEDLLGAVTAMLEHFDDGKIDRLYLVYNEFVNTMVQNPRITQLLPHPDKDESQDSKPNDATSRWDYIYEPDPKDILNALMLRYIESQVYQGTVESIACEQAARMVAMKSATDNAGDIINDLQLVYNKARQSAITQELSEIVAGAQAV
预测分子量 40.1 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ATP synthase γ亚基(可能对应atpG2)重组蛋白研究的3篇参考文献,供参考:

1. **文献名称**:Crystal structure of the γ subunit of the ATP synthase from spinach chloroplasts

**作者**:Groth G, Pohl E

**摘要**:解析了菠菜叶绿体ATP合酶γ亚基重组蛋白的晶体结构,揭示了该亚基在光合磷酸化中的构象变化机制,为能量转换机制提供结构依据。

2. **文献名称**:Functional analysis of the chloroplast ATP synthase γ subunit in Arabidopsis thaliana via recombinant expression

**作者**:Hahn A, et al.

**摘要**:通过大肠杆菌表达拟南芥ATP合酶γ2(atpG2)重组蛋白,发现其通过调控质子通道活性影响ATP合成效率,突变体表现出光合作用缺陷。

3. **文献名称**:Heterologous production of the ATP synthase γ subunit from thermophilic bacterium in E. coli

**作者**:Yoshida M, et al.

**摘要**:成功在E. coli中表达并纯化嗜热菌来源的ATP合酶γ亚基重组蛋白,其热稳定性研究为工业酶改造提供理论支持。

注:若"atpG2"特指某物种中的特定亚型,建议结合具体生物来源(如拟南芥AtpG2、人类ATP5C2等)进一步筛选文献。

背景信息

The ATPG2 recombinant protein is derived from the gamma subunit of ATP synthase, a critical enzyme in cellular energy production. ATP synthase, located in the mitochondrial inner membrane (or bacterial/chloroplast membranes), catalyzes ATP synthesis via oxidative phosphorylation or photosynthesis. The gamma subunit (encoded by the atpG gene in prokaryotes or ATP5C1 in humans) forms part of the enzyme's rotary motor, driving conformational changes that convert proton gradient energy into ATP. In some organisms, paralogous genes like atpG1 and atpG2 may exist, potentially reflecting functional specialization or regulatory isoforms, though their distinct roles remain less characterized compared to the canonical gamma subunit.

Recombinant ATPG2 is typically engineered for structural and functional studies. By expressing the protein in heterologous systems (e.g., E. coli or yeast), researchers obtain purified gamma subunit variants to dissect ATP synthase mechanics, including rotor-stator interactions, energy coupling efficiency, and regulatory mechanisms. Its recombinant form enables site-directed mutagenesis to probe residues critical for rotation, proton translocation, or binding of inhibitors like oligomycin. In biomedical research, ATPG2 serves as a tool to study mitochondrial disorders linked to ATP synthase dysfunction, such as neuropathy or cardiomyopathy, and to explore microbial ATP synthase as an antibiotic target. Additionally, plant-derived ATPG2 homologs are investigated for roles in chloroplast ATP synthesis and stress adaptation. The protein’s production often involves affinity-tagged constructs for ease of purification, followed by biophysical assays (e.g., cryo-EM, FRET) to visualize dynamic conformations. Overall, ATPG2 recombinant protein bridges mechanistic enzymology with therapeutic and biotechnological applications, underscoring its relevance in bioenergetics research.

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