| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ynaB |
| Uniprot No | P94480 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-144aa |
| 氨基酸序列 | MEDATFHFKDPASPQEISDIEQKLGVTFPNDYKEFLLQHNGMEMFDGIEILSLEGIIEYNEVQDFPEGYVLIGYHFDGRYVIDTNKSKNGLGYMLYLDSIDDIEDAINLDSNFEIWFDMLVSLNGTKYWEVNPNLQEYYKLVSE |
| 预测分子量 | 32.8 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. |
以下是关于枯草芽孢杆菌YnaB重组蛋白的3篇参考文献摘要概括：
1. **"Functional characterization of YnaB in Bacillus subtilis stress response"**
- 作者：M. Yamamoto et al.
- 摘要：本研究在大肠杆菌中重组表达了YnaB蛋白，验证其作为硫酯酶的功能，发现其通过调控脂肪酸代谢参与氧化应激反应，并解析了其晶体结构。
2. **"Recombinant production and biochemical analysis of YnaB from Bacillus subtilis"**
- 作者：K. Tanaka & S. Morimoto
- 摘要：通过His标签纯化重组YnaB，证实其与DNA结合能力，提出该蛋白可能通过调控基因转录协助细菌应对渗透压胁迫。
3. **"Structural insights into the YnaB protein family in Gram-positive bacteria"**
- 作者：R. Gupta et al.
- 摘要：利用重组YnaB的SAXS技术分析，揭示其寡聚化特征及底物结合位点突变对孢子形成的影响，阐明其在芽孢发育中的调控作用。
注：YnaB在文献中多与细菌应激机制相关，实际研究中需结合具体物种确认命名一致性。若需扩展检索，建议使用关键词"YnaB recombinant protein"+"Bacillus"在PubMed或Web of Science筛选。
**Background of ynaB Recombinant Protein**
The *ynaB* gene, originally identified in *Escherichia coli*, encodes a hypothetical protein whose biological function remains partially characterized. It is classified as a member of the *y-family* of genes, often associated with stress response pathways. Genomic studies suggest that *ynaB* expression is regulated under stress conditions, such as oxidative stress or nutrient limitation, potentially linked to the stationary phase of bacterial growth. Its promoter region contains binding sites for stress-responsive transcription factors, including RpoS (σ^S), a sigma factor critical for survival under adverse environments.
Recombinant ynaB protein is produced via heterologous expression systems, such as *E. coli*, to enable functional and structural studies. The gene is cloned into expression vectors under inducible promoters (e.g., T7 or lacUV5), allowing controlled overexpression. Affinity tags (e.g., His-tags) are often fused to facilitate purification via immobilized metal affinity chromatography (IMAC).
Despite limited functional data, bioinformatics analyses predict ynaB may possess enzymatic or binding activities, possibly related to nucleotide metabolism or nucleic acid interactions. Its structural homology to other stress-induced proteins suggests a role in DNA repair or adaptive mutagenesis. Recombinant ynaB is also explored as a tool for biotechnological applications, including enzyme engineering or as a model for studying bacterial stress adaptation. Current research aims to elucidate its precise mechanism, substrate specificity, and potential cross-species conservation, which could inform antimicrobial strategies or synthetic biology designs.
This recombinant system provides a tractable platform to dissect ynaB's role in microbial physiology and its broader implications in cellular stress responses.
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