| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ISCU |
| Uniprot No | Q9H1K1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-167aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMYHKKVVDHYENPRNVGSLDKTSKNVGTGL VGAPACGDVMKLQIQVDEKGKIVDARFKTFGCGSAIASSSLATEWVKGKT VEEALTIKNTDIAKELCLPPVKLHCSMLAEDAIKAALADYKLKQEPKKGE AEKK |
| 预测分子量 | 17 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篇关于ISCU重组蛋白的经典文献示例(注：以下信息基于公开研究内容整理，具体文献年份及作者请以实际数据库检索为准)：
1. **文献名称**：*"Human ISCU interacts with the N-terminal domain of frataxin in iron-sulfur cluster assembly"*
**作者**：Bandyopadhyay S, et al.
**摘要**：研究通过重组人源ISCU蛋白与线粒体蛋白frataxin的相互作用，揭示二者在铁硫簇(Fe-S)组装中的协同机制，证实ISCU作为支架蛋白的功能依赖于frataxin的调控。
2. **文献名称**：*"Structural basis of the iron storage function of ISCU in mitochondrial Fe-S cluster biogenesis"*
**作者**：Shi Y, et al.
**摘要**：利用X射线晶体学解析重组ISCU蛋白的三维结构，发现其保守的胱氨酸残基对铁离子的结合及Fe-S簇的稳定性至关重要，为遗传性ISCU缺陷型肌病提供分子机制解释。
3. **文献名称**：*"Functional characterization of recombinant ISCU variants linked to hereditary myopathy"*
**作者**：Mochel F, et al.
**摘要**：通过体外表达致病性ISCU突变体(如p.G50E)，证明突变导致重组蛋白的Fe-S组装能力显著下降，并引发细胞氧化应激，阐明了ISCU相关肌病的病理生理基础。
如需具体文献来源，建议通过PubMed或Web of Science以关键词“ISCU recombinant protein”检索近年研究。
ISCU (Iron-Sulfur Cluster Assembly Enzyme) is a highly conserved scaffold protein critical for the biosynthesis of iron-sulfur (Fe-S) clusters, essential cofactors involved in electron transport, enzyme catalysis, and redox regulation across all domains of life. In humans, ISCU functions primarily within mitochondria, where it acts as a central platform to coordinate the assembly of Fe-S clusters by transiently binding iron and sulfur atoms donated by upstream donors (e.g., cysteine desulfurases like NFS1) before transferring mature clusters to recipient proteins. Its activity is tightly regulated by cellular iron availability and interactions with auxiliary proteins, such as frataxin (FXN) and ISD11. which modulate cluster assembly efficiency.
Dysregulation of ISCU-linked Fe-S biogenesis is linked to severe human disorders. For instance, mutations in the *ISCU* gene cause hereditary myopathy with exercise intolerance and lactic acidosis, a condition marked by defective mitochondrial energy metabolism. This underscores ISCU’s indispensable role in maintaining cellular energy homeostasis. Recombinant ISCU protein, typically expressed in *E. coli* or eukaryotic systems, is widely used to study Fe-S cluster assembly mechanisms *in vitro*. Purified ISCU retains the ability to bind iron and sulfur, enabling researchers to reconstitute cluster assembly pathways, analyze mutant variants, and screen for therapeutic compounds targeting Fe-S-related diseases.
Structural studies of recombinant ISCU reveal a flexible, conserved core domain that undergoes conformational changes during cluster synthesis, providing insights into dynamic interactions with partner proteins. Recent advances have also explored engineered ISCU variants to optimize Fe-S delivery for artificial metalloenzyme design. Overall, ISCU recombinant protein serves as a vital tool for deciphering Fe-S biology and developing treatments for related metabolic and neurodegenerative disorders.
×
