| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPK1 |
| Uniprot No | Q9H3S4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-243aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMEHAFT PLEPLLSTGN LKYCLVILNQ PLDNYFRHLW NKALLRACAD GGANRLYDIT EGERESFLPE FINGDFDSIR PEVREYYATK GCELISTPDQ DHTDFTKCLK MLQKKIEEKD LKVDVIVTLG GLAGRFDQIM ASVNTLFQAT HITPFPIIII QEESLIYLLQ PGKHRLHVDT GMEGDWCGLI PVGQPCMQVT TTGLKWNLTN DVLAFGTLVS TSNTYDGSGV VTVETDHPLL WTMAIKS |
| 预测分子量 | 30 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TPK1重组蛋白的模拟参考文献示例(文献信息为虚构，仅供示例参考)：
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1. **"Expression and Functional Characterization of Recombinant TPK1 in Saccharomyces cerevisiae"**
*Authors: A. Smith et al.*
摘要：本研究报道了酿酒酵母中TPK1重组蛋白的高效表达与纯化，分析了其cAMP依赖性激酶活性，并证实其在细胞代谢调控中的关键作用。
2. **"Structural Insights into Human TPK1 Kinase Domain by X-ray Crystallography"**
*Authors: B. Lee, C. Zhang*
摘要：通过X射线晶体学解析了人源TPK1激酶结构域的3D结构，揭示了ATP结合口袋的构象特征，为靶向药物设计提供了结构基础。
3. **"TPK1 Recombinant Protein Enhances Neuronal Differentiation in vitro"**
*Authors: M. Chen et al.*
摘要：利用哺乳动物细胞系统表达TPK1重组蛋白，发现其通过激活CREB信号通路显著促进神经干细胞的分化，提示其在神经再生中的潜在应用。
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**注**：以上文献为模拟创作，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
**Background of TPK1 Recombinant Protein**
TPK1 (Thiamin Pyrophosphokinase 1) is an essential enzyme involved in the biosynthesis of thiamine pyrophosphate (TPP), the active form of vitamin B1 (thiamine). Thiamine is a critical cofactor for central metabolic pathways, including carbohydrate and amino acid metabolism, and plays a vital role in cellular energy production. TPK1 catalyzes the conversion of free thiamine into TPP through ATP-dependent phosphorylation, a step necessary for TPP’s function in enzymes like pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase.
The recombinant TPK1 protein is produced using biotechnological methods, typically through expression in bacterial or mammalian systems, followed by purification to ensure high specificity and activity. Recombinant TPK1 retains the enzymatic properties of the native protein, making it a valuable tool for studying thiamine metabolism, enzymatic kinetics, and interactions with potential inhibitors or activators.
Research on TPK1 has gained attention due to its implications in human health. Mutations or dysregulation of TPK1 are linked to neurological disorders, such as Leigh syndrome and Wernicke-Korsakoff syndrome, which are associated with thiamine deficiency. Additionally, altered TPK1 activity has been observed in certain cancers and metabolic diseases, highlighting its potential as a therapeutic target.
The availability of recombinant TPK1 protein facilitates drug discovery efforts, enabling high-throughput screening for compounds that modulate its activity. It also aids in structural studies, such as X-ray crystallography, to elucidate mechanisms of catalysis and substrate binding. Overall, TPK1 recombinant protein serves as a critical resource for advancing our understanding of thiamine biology and its role in health and disease.
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