| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | msyB |
| Uniprot No | 1-124aa |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-124aa |
| 氨基酸序列 | MTMYATLEEAIDAAREEFLADNPGIDAEDANVQQFNAQKYVLQDGDIMWQVEFFADEGEEGECLPMLSGEAAQSVFDGDYDEIEIRQEWQEENTLHEWDEGEFQLEPPLDTEEGRAAADEWDER |
| 预测分子量 | 16.3 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 **msyB重组蛋白** 的3条参考文献示例(文献信息为虚构，仅作格式参考)：
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1. **文献名称**: *Deletion of msyB Enhances Recombinant Protein Yield in Escherichia coli by Reducing Acetate Accumulation*
**作者**: Tanaka K, et al.
**摘要**: 研究通过删除大肠杆菌中的 **msyB** 基因，发现其可显著降低乙酸代谢副产物的积累，从而改善细胞生长环境，提高重组蛋白(如人胰岛素前体)的表达量和稳定性。
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2. **文献名称**: *MsyB Acts as a Transcriptional Regulator to Optimize Recombinant Protein Expression in Bacillus subtilis*
**作者**: Müller S, et al.
**摘要**: 揭示了 **msyB** 在枯草芽孢杆菌中作为全局转录调控因子的作用，通过抑制竞争性代谢途径基因的表达，优化细胞资源分配，使重组胶原蛋白的产量提升2.3倍。
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3. **文献名称**: *Co-expression of msyB and Chaperones Improves Solubility of Recombinant Antibodies in Yeast*
**作者**: Chen L, et al.
**摘要**: 在毕赤酵母系统中，**msyB** 与分子伴侣(如BiP)共表达可协同减少抗体轻链的错误折叠，显著提高重组抗体的可溶性和活性，为工业化生产提供新策略。
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**备注**：实际研究中，**msyB** 可能涉及代谢调控、压力响应或伴侣功能，建议通过权威数据库(如PubMed)结合关键词检索最新文献。
**Background of msyB Recombinant Protein**
The msyB gene, originally identified in *Mycoplasma* species and other prokaryotic pathogens, encodes a protein associated with bacterial stress responses, virulence, and antibiotic resistance mechanisms. As a member of conserved gene families in microbial genomes, msyB is hypothesized to play roles in nucleic acid binding, metal ion homeostasis, or transcriptional regulation, though its precise molecular function remains under investigation. Recombinant msyB protein is engineered through heterologous expression systems, typically using *E. coli*, to produce purified protein for functional and structural studies.
The production of recombinant msyB involves cloning the gene into expression vectors, optimizing induction conditions (e.g., IPTG or temperature), and employing affinity chromatography (e.g., His-tag purification) to obtain soluble, active protein. This approach enables large-scale production for applications such as crystallography, enzymatic assays, or interaction studies with host cell components. Interest in msyB stems from its potential as a therapeutic target, particularly in combating antibiotic-resistant bacterial infections. For instance, understanding its role in pathogen survival under host immune stress or drug exposure could inform novel antimicrobial strategies.
Additionally, recombinant msyB serves as an antigen for antibody development in diagnostic kits or vaccine research. Challenges include ensuring proper protein folding and stability, as microbial proteins may require specific post-translational modifications or chaperones absent in bacterial expression systems. Despite these hurdles, msyB recombinant protein remains a valuable tool for unraveling microbial pathogenesis and advancing biomedical interventions.
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