纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | TKT |
Uniprot No | P29401 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-623aa |
氨基酸序列 | MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIANIRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLITKA |
预测分子量 | 67.9 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3条关于TKT(转酮醇酶)重组蛋白研究的虚构参考文献示例(仅供学术写作参考格式,非真实文献):
1. **文献名称**: *Heterologous Expression and Characterization of Recombinant Human Transketolase in E. coli*
**作者**: Smith J, et al.
**摘要**: 该研究报道了通过大肠杆菌表达系统高效表达人源TKT重组蛋白的优化策略,分析了纯化蛋白的酶活性和稳定性,为代谢疾病研究提供工具。
2. **文献名称**: *Crystal Structure Analysis of Recombinant Transketolase from Saccharomyces cerevisiae*
**作者**: Chen L, Wang H.
**摘要**: 解析了酵母来源重组TKT蛋白的三维晶体结构,揭示了其底物结合域的关键氨基酸残基,为设计酶活性调节剂奠定结构基础。
3. **文献名称**: *Functional Role of Recombinant TKT in Cancer Cell Metabolism*
**作者**: Gupta R, et al.
**摘要**: 通过体外实验证明,重组TKT蛋白过表达可增强肿瘤细胞磷酸戊糖途径通量,提示其在癌细胞氧化应激耐受中的潜在作用机制。
*注:以上文献为模拟内容,实际引用请通过PubMed/SCI-Hub等平台检索真实文献。*
**Background of Recombinant TKT Protein**
Transketolase (TKT) is a key metabolic enzyme involved in the pentose phosphate pathway (PPP), playing a critical role in linking carbohydrate metabolism to nucleotide biosynthesis and redox balance. It catalyzes the transfer of glycolaldehyde units between sugar phosphates, essential for generating precursors like ribose-5-phosphate (for nucleic acids) and NADPH (for antioxidant defense). Dysregulation of TKT activity has been implicated in various diseases, including diabetes, cancer, and neurodegenerative disorders, making it a target for therapeutic and diagnostic research.
Recombinant TKT protein is produced using genetic engineering techniques, where the TKT gene is cloned into expression vectors and expressed in host systems such as *E. coli*, yeast, or mammalian cells. This approach allows large-scale production of purified, functional TKT for research and industrial applications. Unlike native TKT isolated from tissues, recombinant TKT offers higher purity, consistency, and scalability, while enabling site-specific modifications (e.g., tags for purification or tracking).
Studies leveraging recombinant TKT have advanced understanding of its structure-function relationships, allosteric regulation, and role in disease. For example, TKT overexpression in cancer cells supports rapid proliferation by supplying metabolic intermediates, while its inhibition has been explored as an anticancer strategy. In neurology, TKT variants are linked to rare disorders like Wernicke-Korsakoff syndrome, driving research into enzyme replacement therapies.
Current challenges include optimizing recombinant TKT’s stability and activity, particularly when expressed in prokaryotic systems lacking post-translational modifications. Advances in eukaryotic expression platforms (e.g., insect or mammalian cells) aim to address this, preserving native folding and cofactor binding (e.g., thiamine pyrophosphate). Overall, recombinant TKT remains a vital tool for deciphering metabolic pathways and developing targeted therapies.
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