| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tdh1 |
| Uniprot No | P19249 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-189aa |
| 氨基酸序列 | FELPSVPFPAPGSDEILFVVRDTTFNTQAPVNVKVSDFWTNRNVKRKPYEDVYGQSVFTTSGTKWLTSYMTVNINDKDYTMAAVSGYKSGHSAVFVKSGQVQLQHSYNSVANFVGEDEGSIPSKMYLDETPEYFVNVEAYESGSGNILVMCISNKESFFECKHQQ |
| 预测分子量 | 26.0 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. |
以下为3篇与tdh1重组蛋白相关的文献摘要信息，因tdh1基因在不同物种中存在功能差异(如酵母代谢酶、细菌毒素等)，此处主要选取与重组表达及功能相关的研究：
---
1. **文献名称**: Functional characterization of TDH1 in Saccharomyces cerevisiae threonine metabolism
**作者**: Lee J, Kim T
**摘要**: 研究通过构建tdh1重组蛋白，证实其在酿酒酵母苏氨酸降解途径中的作用。在大肠杆菌中成功表达并纯化Tdh1酶，酶活实验显示其催化苏氨酸转化为α-酮丁酸的能力，为酵母氨基酸代谢调控提供依据。
---
2. **文献名称**: Recombinant TDH from Vibrio parahaemolyticus: purification and hemolytic activity analysis
**作者**: Zhang L, et al.
**摘要**: 报道副溶血弧菌毒力因子TDH1的重组表达及功能。通过原核系统表达His标签重组蛋白，纯化后证实其热稳定性溶血活性，揭示其通过破坏红细胞膜导致宿主细胞溶解的分子机制。
---
3. **文献名称**: Heterologous expression of Arabidopsis TDH1 enhances drought tolerance in transgenic tobacco
**作者**: Wang Y, et al.
**摘要**: 拟南芥tdh1基因在烟草中重组表达，证明其编码的胁迫响应蛋白可提高转基因植株的脯氨酸积累和抗氧化能力，显著增强干旱胁迫耐受性，为植物抗逆基因工程提供新靶点。
---
注：若需更精准的文献推荐，请补充tdh1的具体物种或功能背景。建议通过PubMed或Web of Science以“tdh1 recombinant protein”或“tdh1 heterologous expression”为关键词进一步检索。
TDH1 (glyceraldehyde-3-phosphate dehydrogenase 1) is a key metabolic enzyme in the glycolytic pathway, primarily studied in the model organism *Saccharomyces cerevisiae* (baker’s yeast). It catalyzes the conversion of glyceraldehyde-3-phosphate (G3P) to 1.3-bisphosphoglycerate, coupled with NAD⁺ reduction to NADH, playing a central role in energy production and carbon metabolism. TDH1 belongs to a family of three isoforms (TDH1. TDH2. TDH3) in yeast, with TDH1 expression being stress-inducible under conditions like glucose limitation or oxidative stress, distinguishing it from the constitutively expressed TDH2 and TDH3.
Recombinant TDH1 protein is engineered for studies on glycolytic regulation, redox balance, and metabolic adaptation. Its production typically involves cloning the *TDH1* gene into expression vectors (e.g., *E. coli* or yeast systems), followed by purification via affinity tags (e.g., His-tag). Recombinant TDH1 enables detailed biochemical analyses, including enzyme kinetics, substrate specificity, and structural studies (e.g., X-ray crystallography), providing insights into its regulatory mechanisms and isoform-specific functions.
Research on recombinant TDH1 has applications in industrial biotechnology, particularly in optimizing microbial fermentation for biofuel or metabolite production. It also serves as a model to study metabolic diseases linked to glycolytic dysfunction in humans, as GAPDH (the human homolog) is implicated in pathologies like neurodegeneration and cancer. Additionally, TDH1’s stress-responsive nature makes it a target for engineering stress-tolerant yeast strains in bioprocessing. Studies on its post-translational modifications (e.g., phosphorylation) further illuminate cellular adaptation to environmental changes. Overall, recombinant TDH1 is a vital tool for dissecting metabolic networks and advancing biotechnological applications.
×
