| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | hchA |
| Uniprot No | P31658 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-283aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMTVQTSKNPQVDIAEDNAFFPSEYSLSQYT SPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLL PLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNP KKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRF VISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWY FGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAA YAG |
| 预测分子量 | 33 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hchA重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "The hchA gene of Escherichia coli encodes a stress response protein involved in chaperone-mediated protein aggregation control"
**作者**: Ishii, A., et al.
**摘要**: 研究揭示hchA编码的蛋白在大肠杆菌中参与调控蛋白聚集，尤其在热应激条件下与σ因子RpoH相互作用，重组hchA蛋白在体外抑制错误折叠蛋白的聚集，表明其分子伴侣功能。
2. **文献名称**: "Expression and purification of recombinant HchA from Pseudomonas aeruginosa and its role in oxidative stress tolerance"
**作者**: Zhang, L., & Wang, Q.
**摘要**: 报道铜绿假单胞菌hchA重组蛋白的高效表达及纯化方法，证实HchA通过调节抗氧化酶活性增强细菌对H₂O₂的抗性，为研究其抗氧化机制提供基础。
3. **文献名称**: "Structural and functional characterization of HchA in Bacillus subtilis: A novel protease-associated stress adaptor"
**作者**: Müller, R., et al.
**摘要**: 解析枯草芽孢杆菌HchA重组蛋白的晶体结构，发现其N端结构域与蛋白酶降解异常蛋白相关，敲除hchA导致细菌在高温下生长缺陷，提示其在胁迫适应中的关键作用。
注：上述文献为虚拟示例，实际研究中建议通过PubMed或Web of Science以关键词“hchA recombinant”检索最新论文。
The hchA gene, originally identified in Escherichia coli, encodes a protein involved in bacterial stress response pathways, particularly under conditions of protein misfolding or oxidative stress. HchA (also known as Hsp31 or YedU) belongs to the DJ-1/ThiJ/PfpI superfamily and functions as a molecular chaperone and protease, playing a critical role in mitigating cellular damage during environmental stress. It is induced during the stationary phase and under heat shock, helping bacteria survive adverse conditions by preventing protein aggregation or degrading irreversibly damaged proteins.
Recombinant hchA protein is produced through genetic engineering, typically by cloning the hchA gene into expression vectors (e.g., plasmid systems in E. coli), followed by induction with IPTG or temperature shifts. Purification methods often involve affinity chromatography using His-tags or other fusion tags. The recombinant protein retains its native chaperone and enzymatic activities, making it a valuable tool for studying bacterial stress adaptation mechanisms.
Research on hchA has implications for understanding microbial survival strategies in hostile environments, including antibiotic exposure or host immune responses. Its structural and functional characterization aids in exploring evolutionary conservation across species, as homologs exist in pathogens like Salmonella and Pseudomonas. Additionally, hchA's role in protein quality control has sparked interest in biotechnological applications, such as improving microbial fermentation resilience or developing novel antimicrobial strategies targeting stress-response pathways. Studies also investigate its potential cross-talk with other chaperones like GroEL/ES or DnaK, providing insights into redundant stress-management networks in prokaryotes.
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