| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MOSC1 |
| Uniprot No | Q5VT66 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-337aa |
| 氨基酸序列 | MGAAGSSALARFVLLAQSRPGWLGVAALGLTAVALGAVAWRRAWPTRRRRLLQQVGTVAQLWIYPVKSCKGVPVSEAECTAMGLRSGNLRDRFWLVINQEGNMVTARQEPRLVLISLTCDGDTLTLSAAYTKDLLLPIKTPTTNAVHKCRVHGLEIEGRDCGEATAQWITSFLKSQPYRLVHFEPHMRPRRPHQIADLFRPKDQIAYSDTSPFLILSEASLADLNSRLEKKVKATNFRPNIVISGCDVYAEDSWDELLIGDVELKRVMACSRCILTTVDPDTGVMSRKEPLETLKSYRQCDPSERKLYGKSPLFGQYFVLENPGTIKVGDPVYLLGQ |
| 预测分子量 | 37,4 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MOSC1重组蛋白的3篇参考文献示例(注：文献为模拟示例，实际研究中请核实具体文献)：
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1. **文献名称**: *Structural insights into MOSC1-mediated mitochondrial tRNA cysteine acylation*
**作者**: Agris, P.F. et al.
**摘要**: 研究通过重组表达纯化的MOSC1蛋白，解析其晶体结构，揭示其在线粒体半胱氨酸-tRNA合成中的催化机制及底物结合特性。
2. **文献名称**: *Functional characterization of recombinant MOSC1 in oxidative stress response*
**作者**: Hotopp, J.C. et al.
**摘要**: 利用重组MOSC1蛋白进行体外实验，证明其通过调控硫代谢通路减轻细胞氧化损伤，并探讨其与神经退行性疾病的相关性。
3. **文献名称**: *Recombinant MOSC1 expression and enzymatic activity analysis in bacterial systems*
**作者**: Shibata, S. et al.
**摘要**: 报道在大肠杆菌中高效表达可溶性MOSC1重组蛋白的方法，并验证其氨基酰化酶活性，为功能研究提供工具。
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**备注**：
- 若实际文献不足，建议扩展关键词(如“MOSC1 mitochondrial enzyme”或“CARS2”，因MOSC1可能对应特定基因别名)。
- 可结合数据库(如UniProt、PubMed)或综述类文献追踪相关研究。
MOSC1 (Molybdenum Cofactor Sulfurase 1) is a critical enzyme involved in the biosynthesis of the molybdenum cofactor (Moco), an essential prosthetic group required for the activity of molybdenum-dependent enzymes such as sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. Moco-containing enzymes play vital roles in cellular redox reactions, detoxification, and metabolic pathways. MOSC1. also known as MOCS3 or gephyrin-like protein, functions as a sulfurase that transfers sulfur to the molybdenum cofactor precursor, a key step in Moco maturation. This post-translational modification ensures proper enzymatic function across diverse biological systems.
Recombinant MOSC1 protein is engineered using expression systems like *E. coli* or mammalian cells to enable large-scale production for functional and structural studies. Its recombinant form retains the ability to bind substrates and catalyze sulfur transfer, making it invaluable for *in vitro* assays investigating Moco biosynthesis defects linked to human disorders. Mutations in MOSC1 or related Moco synthesis genes can cause severe metabolic diseases, such as molybdenum cofactor deficiency (MoCD), a rare autosomal recessive condition characterized by neurological impairments and early lethality.
Research on recombinant MOSC1 has advanced understanding of sulfur mobilization in cofactor assembly and its interplay with other enzymes in the Moco pathway. It also serves as a tool for drug discovery targeting Moco-related disorders or for engineering Moco-dependent enzymes in biotechnology. Structural studies using recombinant MOSC1 have revealed insights into its dual-domain architecture, including a N-terminal domain for substrate recognition and a C-terminal rhodanese-like domain responsible for sulfur transfer. These findings underscore its evolutionary conservation and mechanistic role in cellular metabolism.
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