| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | talB |
| Uniprot No | P0A870 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-317aa |
| 氨基酸序列 | TDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL |
| 预测分子量 | 42.5 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talB重组蛋白的3篇参考文献概览：
1. **文献名称**：*Cloning and overexpression of the talB gene encoding transaldolase from Escherichia coli*
**作者**：Sprenger GA, Sahm H
**摘要**：该研究报道了大肠杆菌talB基因的克隆及其在高表达载体中的重组表达。通过优化表达条件，成功获得高活性转醛酶，并验证其在磷酸戊糖途径中的功能。
2. **文献名称**：*Characterization of recombinant transaldolase (talB) in metabolic engineering applications*
**作者**：Zhao J, Shimizu K
**摘要**：研究分析了重组talB蛋白在代谢工程中的潜力，发现其过表达可增强微生物的NADPH供应能力，为优化生物合成途径(如芳香族化合物)提供理论支持。
3. **文献名称**：*Crystallization and structural analysis of Escherichia coli transaldolase B*
**作者**：Marx A, et al.
**摘要**：通过重组talB蛋白的结晶和X射线衍射分析，揭示了该酶的三维结构及底物结合位点，为理性设计酶突变体以提升催化效率奠定基础。
注：以上文献信息为示例，实际引用需根据具体论文内容调整。建议通过PubMed或Web of Science以“talB recombinant protein”、“transaldolase expression”为关键词检索最新文献。
**Background of talB Recombinant Protein**
The talB gene encodes transaldolase, a key enzyme in the pentose phosphate pathway (PPP), which plays a critical role in cellular metabolism by balancing carbon flux between glycolysis and nucleotide biosynthesis. Transaldolase catalyzes the reversible transfer of a dihydroxyacetone group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, generating erythrose-4-phosphate and fructose-6-phosphate. This reaction is essential for maintaining metabolic flexibility, particularly in rapidly dividing cells or under oxidative stress. Dysregulation of transaldolase activity has been linked to metabolic disorders, cancer, and immune dysfunction, highlighting its biological significance.
Recombinant talB protein is produced through heterologous expression systems, such as *E. coli* or yeast, enabling large-scale purification for functional and structural studies. The recombinant form retains enzymatic activity and stability, making it a valuable tool for *in vitro* assays, substrate specificity investigations, and inhibitor screening. Its production often involves cloning the talB gene into expression vectors with affinity tags (e.g., His-tag) to facilitate purification via chromatography.
Research on talB recombinant protein has advanced understanding of PPP regulation and its interplay with other metabolic pathways. It also serves as a potential therapeutic target; for instance, inhibiting transaldolase in cancer cells could disrupt nucleotide synthesis, impairing tumor growth. Additionally, structural studies using recombinant talB have elucidated catalytic mechanisms and guided drug design. Beyond biomedical applications, this enzyme is utilized in industrial biotechnology for synthesizing rare sugars or metabolic engineering of microbial strains.
Overall, talB recombinant protein bridges fundamental biochemistry with translational research, offering insights into metabolic diseases and biotechnological innovations.
×
