纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | IHPK1 |
Uniprot No | Q92551 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-441aa |
氨基酸序列 | MCVCQTMEVGQYGKNASRAGDRGVLLEPFIHQVGGHSSMMRYDDHTVCKP LISREQRFYESLPPEMKEFTPEYKGVVSVCFEGDSDGYINLVAYPYVESE TVEQDDTTEREQPRRKHSRRSLHRSGSGSDHKEEKASLSLETSESSQEAK SPKVELHSHSEVPFQMLDGNSGLSSEKISHNPWSLRCHKQQLSRMRSESK DRKLYKFLLLENVVHHFKYPCVLDLKMGTRQHGDDASAEKAARQMRKCEQ STSATLGVRVCGMQVYQLDTGHYLCRNKYYGRGLSIEGFRNALYQYLHNG LDLRRDLFEPILSKLRGLKAVLERQASYRFYSSSLLVIYDGKECRAESCL DRRSEMRLKHLDMVLPEVASSCGPSTSPSNTSPEAGPSSQPKVDVRMIDF AHSTFKGFRDDPTVHDGPDRGYVFGLENLISIMEQMRDENQ |
预测分子量 | 66 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IHPK1重组蛋白的3篇参考文献摘要,供参考:
1. **"Recombinant human inositol hexakisphosphate kinase 1 (IHPK1) production and biochemical characterization"**
- 作者:Smith A, et al.
- 摘要:该研究描述了IHPK1重组蛋白在大肠杆菌中的高效表达与纯化方法,分析了其酶活性及对肌醇多磷酸代谢的影响,为后续功能研究提供工具。
2. **"Structural insights into IHPK1-mediated signaling pathways using recombinant protein crystallography"**
- 作者:Zhang L, et al.
- 摘要:通过重组IHPK1蛋白的晶体结构解析,揭示了其底物结合域和催化机制,探讨了其在细胞增殖和凋亡调控中的潜在作用。
3. **"IHPK1 deficiency alters T cell metabolism: Evidence from recombinant protein-based assays"**
- 作者:Chen H, et al.
- 摘要:利用重组IHPK1蛋白进行体外实验,发现其通过调节肌醇磷酸代谢影响T细胞能量代谢,可能成为免疫治疗的新靶点。
注:以上文献信息为模拟示例,实际文献需通过PubMed或Web of Science等平台检索确认。
IHPK1 (Inositol Hexakisphosphate Kinase 1) is an enzyme encoded by the *IP6K1* gene, primarily involved in the metabolism of inositol phosphates, a group of signaling molecules critical for cellular processes. It catalyzes the conversion of inositol hexakisphosphate (IP6) to 5-diphospho-inositol pentakisphosphate (IP7), a high-energy phosphate donor that regulates diverse functions, including apoptosis, DNA repair, and vesicular trafficking. Dysregulation of IHPK1 has been linked to metabolic disorders, neurodegenerative diseases, and cancer, making it a potential therapeutic target.
Recombinant IHPK1 protein is produced through genetic engineering, typically by expressing the *IP6K1* gene in bacterial (e.g., *E. coli*) or mammalian cell systems. This allows large-scale production of purified, functional IHPK1 for research applications. The recombinant protein retains enzymatic activity, enabling studies on its kinetic properties, substrate specificity, and interaction with inhibitors or modulators. Its structure often includes affinity tags (e.g., His-tag) for simplified purification and detection.
Research using recombinant IHPK1 has advanced understanding of its role in cellular signaling networks. For example, IP7 generated by IHPK1 influences insulin secretion by regulating exocytosis in pancreatic β-cells, suggesting implications for diabetes. In cancer, elevated IHPK1 activity may promote tumor growth via metabolic reprogramming. Additionally, IP7’s involvement in neuronal function highlights its relevance to conditions like Alzheimer’s disease. Recombinant IHPK1 also facilitates drug discovery, serving as a tool to screen small molecules targeting its catalytic site. However, challenges remain in elucidating tissue-specific functions and optimizing selective inhibitors. Overall, recombinant IHPK1 is a vital resource for both basic research and translational studies aiming to exploit inositol phosphate pathways for therapeutic interventions.
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