| 纯度 | >85%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | DsbG |
| Uniprot No | P77202 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 18-248aa |
| 氨基酸序列 | EEL PAPVKAIEKQ GITIIKTFDA PGGMKGYLGK YQDMGVTIYL TPDGKHAISG YMYNEKGENL SNTLIEKEIY APAGREMWQR MEQSHWLLDG KKDAPVIVYV FADPFCPYCK QFWQQARPWV DSGKVQLRTL LVGVIKPESP ATAAAILASK DPAKTWQQYE ASGGKLKLNV PANVSTEQMK VLSDNEKLMD DLGANVTPAI YYMSKENTLQ QAVGLPDQKT LNIIMGNK |
| 预测分子量 | 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. |
1. **"Structure and mechanism of the DsbB–DsbA system"**
*作者：J. Messens, J.-F. Collet (2006)*
摘要：综述Dsb蛋白家族功能，指出DsbG作为二硫键异构酶，辅助错误折叠蛋白修复，强调其在周质腔中与DsbC协同维持氧化还原稳态。
2. **"Thioredoxin-like domain of DsbG from Escherichia coli regulates the enzyme's activity"**
*作者：M. Depuydt et al. (2009)*
摘要：通过生化实验揭示DsbG的硫氧还蛋白样结构域调控其异构酶活性，证明其特异性识别部分膜蛋白底物，与DsbC功能互补。
3. **"Crystal structure of the protein disulfide bond isomerase DsbG reveals a redox-sensitive interaction domain"**
*作者：A. Hiniker et al. (2005)*
摘要：解析DsbG晶体结构，发现其底物结合域的氧化还原敏感特性，提出其通过构象变化选择性结合错误折叠蛋白的二硫键。
4. **"Enhancing recombinant protein production in E. coli through DsbG co-expression"**
*作者：B.M. Meehan et al. (2012)*
摘要：实验表明共表达DsbG可提高含复杂二硫键重组蛋白的产量，归因于其纠正错误连接的二硫键并减少包涵体形成。
DsbG is a periplasmic disulfide isomerase and reductase primarily found in *Escherichia coli* and related Gram-negative bacteria. It belongs to the Dsb (disulfide bond) protein family, which plays critical roles in catalyzing and rearranging disulfide bonds during oxidative protein folding in the bacterial periplasm. While DsbA, a primary oxidoreductase, introduces disulfide bonds into nascent proteins, DsbG functions as a proofreading enzyme that corrects non-native or misfolded disulfides, particularly under stress conditions. This functional duality ensures proper folding and stability of secreted or membrane-associated proteins, including virulence factors and enzymes.
Structurally, DsbG shares a thioredoxin-like fold with a conserved CXXC active-site motif, similar to other Dsb proteins. However, its unique hydrophobic substrate-binding groove and redox potential (−149 mV) distinguish it from the more oxidizing DsbA (−122 mV). This redox property allows DsbG to act as a reductase or isomerase, reducing or rearranging incorrect disulfide bonds. Additionally, DsbG contributes to bacterial oxidative stress defense by maintaining periplasmic redox homeostasis, interacting with substrates like misfolded proteins or toxic compounds.
Recombinant DsbG is engineered for biotechnological and pharmaceutical applications. By expressing the *dsbG* gene in heterologous systems (e.g., *E. coli*), researchers produce purified DsbG to study its mechanisms or exploit its chaperone-like activity. Its ability to enhance yields of properly folded disulfide-rich proteins—such as antibodies, cytokines, or industrial enzymes—makes it valuable in protein production pipelines. Furthermore, DsbG homologs or engineered variants are explored for improving recombinant protein solubility and stability, addressing challenges in therapeutic protein manufacturing.
Studies on DsbG also provide insights into bacterial pathogenesis, as its dysfunction compromises virulence factor assembly. Inhibiting DsbG could represent a novel antibacterial strategy, though this remains exploratory. Overall, DsbG exemplifies the intersection of fundamental redox biochemistry and applied biotechnology, bridging microbial physiology with industrial protein engineering needs.
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