| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | serB |
| Uniprot No | P78330 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-225aa |
| 氨基酸序列 | MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE |
| 预测分子量 | 25 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serB重组蛋白的3条示例参考文献(内容为模拟概括，非真实文献)：
1. **标题**：Cloning and functional characterization of serB phosphatase in *E. coli*
**作者**：Smith A, et al.
**期刊**：Appl Microbiol Biotechnol (2005)
**摘要**：报道了serB基因在大肠杆菌中的重组表达与纯化，验证了其磷酸丝氨酸磷酸酶活性，并优化了反应条件以提高酶稳定性。
2. **标题**：Structural insights into serB enzyme mechanism by X-ray crystallography
**作者**：Chen L, et al.
**期刊**：J Struct Biol (2012)
**摘要**：通过X射线晶体学解析了重组serB蛋白的三维结构，揭示了其催化位点关键氨基酸残基，为设计靶向抑制剂提供依据。
3. **标题**：serB as a novel biocatalyst for industrial L-serine production
**作者**：Yamamoto K, et al.
**期刊**：Biotechnol J (2018)
**摘要**：开发了基于重组serB蛋白的固定化酶系统，显著提升了L-丝氨酸的生物合成效率，展示了其在工业发酵中的应用潜力。
注：以上为模拟文献，实际引用时建议通过PubMed/Google Scholar检索真实文献(关键词：serB recombinant protein, phosphoserine phosphatase)。
**Background of SerB Recombinant Protein**
SerB, or phosphoserine phosphatase, is a key enzyme involved in serine biosynthesis, catalyzing the dephosphorylation of phosphoserine to produce serine. This reaction represents the final step in the phosphorylated pathway of serine synthesis, which is critical for cellular metabolism, particularly in organisms that cannot acquire sufficient serine from external sources. In bacteria like *Salmonella enterica*, SerB (encoded by the *serB* gene) is essential for survival under serine-limiting conditions and has been implicated in virulence and stress adaptation.
The recombinant SerB protein is typically produced through heterologous expression in bacterial host systems, such as *Escherichia coli*, using plasmid vectors that enable high-yield protein production. The gene encoding SerB is cloned into an expression vector, often fused with affinity tags (e.g., His-tag) to facilitate purification via chromatography. Recombinant SerB retains its enzymatic activity, making it valuable for biochemical studies, including substrate specificity, kinetic analysis, and inhibitor screening.
Interest in SerB extends beyond its metabolic role. In pathogenic bacteria, SerB has been explored as a potential vaccine candidate or antimicrobial target due to its contribution to pathogenicity. For example, *Salmonella* SerB is immunogenic and has been studied in subunit vaccine development. Additionally, structural studies of recombinant SerB have provided insights into its catalytic mechanism, aiding the design of small-molecule inhibitors.
The production of recombinant SerB also supports applications in enzymology, molecular biology, and drug discovery, offering a purified, well-characterized tool to investigate serine biosynthesis pathways or develop novel antibacterial strategies. Its role in bridging primary metabolism and pathogenicity underscores its biological and therapeutic significance.
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