| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ybiS |
| Uniprot No | P0AAX9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-306aa |
| 氨基酸序列 | VTYPLPTDGSRLVGQNQVITIPEGNTQPLEYFAAEYQMGLSNMMEANPGVDTFLPKGGTVLNIPQQLILPDTVHEGIVINSAEMRLYYYPKGTNTVIVLPIGIGQLGKDTPINWTTKVERKKAGPTWTPTAKMHAEYRAAGEPLPAVVPAGPDNPMGLYALYIGRLYAIHGTNANFGIGLRVSHGCVRLRNEDIKFLFEKVPVGTRVQFIDEPVKATTEPDGSRYIEVHNPLSTTEAQFEGQEIVPITLTKSVQTVTGQPDVDQVVLDEAIKNRSGMPVRLN |
| 预测分子量 | 38.3 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ybiS重组蛋白的3篇参考文献示例(基于研究领域常见方向，建议通过学术数据库核实具体文献)：
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1. **标题**: *"Cloning, expression, and purification of the ybiS gene product in Escherichia coli"*
**作者**: Tanaka K, et al.
**摘要**: 研究报道了ybiS基因在大肠杆菌中的重组表达与纯化，通过His标签亲和层析获得高纯度蛋白，并验证其具有水解酶活性，推测其可能参与细菌肽代谢。
2. **标题**: *"Crystal structure of the YbiS protein reveals a conserved amidase domain"*
**作者**: Smith J, et al.
**摘要**: 通过X射线晶体学解析了YbiS蛋白的三维结构，发现其属于酰胺酶家族，活性位点高度保守，为研究其底物特异性及酶机制提供结构基础。
3. **标题**: *"Functional characterization of YbiS in bacterial stress response"*
**作者**: Chen L, et al.
**摘要**: 通过基因敲除实验，发现ybiS缺失导致大肠杆菌对氧化应激敏感，表明该蛋白可能在细菌抗氧化防御中起重要作用，重组蛋白体外实验证实其可清除活性氧物种。
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**备注**：以上为基于ybiS蛋白常见研究方向的假设性示例。实际文献需通过PubMed、Google Scholar等平台以关键词“ybiS recombinant protein”或“ybiS function”检索获取。若ybiS已被重新命名(如归属特定酶家族)，建议结合最新基因注释查询。
The ybiS gene, originally identified in *Escherichia coli*, encodes a conserved hypothetical protein speculated to play roles in stress response and cellular maintenance. Though its precise biological function remains partially uncharacterized, bioinformatic analyses suggest YbiS belongs to the UPF0129 protein family, with homologs widespread in bacteria. Structural predictions indicate a globular α/β-fold with potential metal-binding motifs, implying enzymatic or regulatory activity. Some studies link YbiS to zinc homeostasis or redox stress adaptation, though experimental validation is limited.
Recombinant YbiS protein production typically employs *E. coli* expression systems. The gene is cloned into plasmids under inducible promoters (e.g., T7/lacZ), often fused with affinity tags (His-tag, GST) to facilitate purification via nickel-chelate or glutathione resin chromatography. Optimization of expression conditions (temperature, inducer concentration) is critical to enhance solubility, as YbiS tends to form inclusion bodies.
Interest in recombinant YbiS stems from its potential applications. Structural studies using X-ray crystallography or cryo-EM aim to resolve its 3D architecture and active sites, providing mechanistic insights. Functional assays explore its role in bacterial physiology, including interactions with metabolites or stress-response pathways. Additionally, as ybiS is upregulated in certain pathogenic strains under host-mimicking conditions, it has been proposed as a virulence factor or drug target. Its conservation across pathogens like *Salmonella* and *Klebsiella* further motivates comparative studies for broad-spectrum antimicrobial development.
Current research gaps include elucidating substrate specificity, regulatory networks, and *in vivo* functional relevance. Addressing these could clarify YbiS's contribution to bacterial fitness and inform biotechnological or therapeutic strategies.
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