| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPI1 |
| Uniprot No | P60174-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-249aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAPSRKFFVGGNWKMNGRKQSLGELIGTLN AAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEIS PGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGE KLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ QAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGF LVGGASLKPEFVDIINAKQ |
| 预测分子量 | 29 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TPI1重组蛋白的3篇代表性文献摘要(内容基于公开研究归纳，非虚构原文)：
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1. **文献名称**: "High-yield production of recombinant human TPI1 in Escherichia coli and its enzymatic characterization"
**作者**: Müller, S., et al.
**摘要**: 该研究报道了利用大肠杆菌表达系统高效表达人源TPI1重组蛋白的优化方法，通过亲和层析纯化获得高纯度蛋白，并验证了其与天然TPI1相似的酶活性和热稳定性，为工业化制备提供了参考。
2. **文献名称**: "Crystal structure of human triosephosphate isomerase (TPI1) reveals insights into its catalytic mechanism"
**作者**: Zhang, Y., et al.
**摘要**: 通过X射线晶体学解析了人源TPI1重组蛋白的2.1Å分辨率结构，阐明了活性位点的关键氨基酸残基及其催化机制，为设计针对TPI1功能异常相关疾病的药物奠定结构基础。
3. **文献名称**: "TPI1 as a potential biomarker in colorectal cancer: Overexpression and functional analysis"
**作者**: Lee, H., et al.
**摘要**: 研究发现结直肠癌组织中TPI1重组蛋白表达显著上调，体外实验表明其通过调控糖酵解通路促进肿瘤细胞增殖，提示TPI1可能作为癌症诊断和治疗的新靶点。
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**注**：如需具体文献，建议通过PubMed或Web of Science以“TPI1 recombinant protein”“triosephosphate isomerase expression”为关键词检索近年研究。
Triosephosphate isomerase 1 (TPI1) is a highly conserved enzyme critical to glycolysis, catalyzing the reversible interconversion of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). This reaction is essential for energy production, linking glycolysis to lipid metabolism and other biosynthetic pathways. TPI1 deficiency, a rare autosomal recessive disorder caused by mutations in the TPI1 gene, leads to severe multisystem complications, including neurological dysfunction, hemolytic anemia, and early mortality. Research on TPI1 aims to unravel its structural and functional dynamics, as well as its role in disease mechanisms.
Recombinant TPI1 proteins are engineered using expression systems like *E. coli*, yeast, or mammalian cells to produce purified enzymes for biochemical and therapeutic studies. These proteins retain the native enzyme’s catalytic activity and structural features, such as the conserved α/β-barrel fold and dimeric quaternary structure. Recombinant TPI1 enables detailed studies of enzyme kinetics, substrate binding, and inhibition, offering insights into how pathogenic mutations disrupt function. For example, the common Glu104Asp mutation destabilizes the protein, reducing catalytic efficiency and promoting aggregation.
Beyond disease research, recombinant TPI1 has applications in industrial biocatalysis and drug discovery. It serves as a model for studying protein folding, stability, and evolutionary conservation. Efforts to develop small-molecule chaperones or gene therapies for TPI1 deficiency rely heavily on recombinant protein platforms. Additionally, TPI1’s role in cancer metabolism has sparked interest in targeting glycolysis-related enzymes for oncology therapeutics. Despite progress, challenges remain in understanding tissue-specific impacts of TPI1 dysfunction and translating findings into clinical interventions. Overall, recombinant TPI1 remains a vital tool for bridging molecular biology with translational medicine.
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