| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MOCS2 |
| Uniprot No | O96007 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-188aa |
| 氨基酸序列 | MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMSSLEISSSCFSLE TKLPLSPPLVEDSAFEPSRKDMDEVEEKSKDVINFTAEKLSVDEVSQLVI SPLCGAISLFVGTTRNNFEGKKVISLEYEAYLPMAENEVRKICSDIRQKW PVKHIAVFHRLGLVPVSEASIIIAVSSAHRAASLEAVSYAIDTLKAKVPI WKKEIYEESSTWKGNKECFWASNS |
| 预测分子量 | 25 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MOCS2重组蛋白的参考文献示例(内容为虚构，仅供格式参考)：
1. **文献名称**：*Recombinant expression and functional characterization of human MOCS2 in Escherichia coli*
**作者**：Zhang L, et al.
**摘要**：研究通过在大肠杆菌中成功表达并纯化重组MOCS2蛋白，验证其参与钼辅因子合成的酶活性，为体外研究钼辅因子缺乏症提供了工具。
2. **文献名称**：*Structural insights into the MOCS2 complex: Implications for molybdenum cofactor biosynthesis*
**作者**：Smith J, et al.
**摘要**：利用X射线晶体学解析MOCS2重组蛋白的三维结构，揭示其与MOCS3相互作用的关键位点，阐明了钼辅因子合成的分子机制。
3. **文献名称**：*Optimization of MOCS2 recombinant protein production in mammalian cells for therapeutic applications*
**作者**：Wang Y, et al.
**摘要**：在HEK293细胞中优化MOCS2重组蛋白表达条件，证明其生物活性可用于钼辅因子替代疗法的临床前研究。
4. **文献名称**：*A high-throughput assay for MOCS2-dependent molybdopterin synthesis using purified recombinant components*
**作者**：Garcia R, et al.
**摘要**：开发基于重组MOCS2蛋白的体外高效酶活检测体系，为钼辅因子相关疾病的药物筛选提供了平台。
**注**：以上文献为示例模板，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“MOCS2 recombinant protein”获取。
**Background of MOCS2 Recombinant Protein**
MOCS2 (Molybdenum Cofactor Synthesis 2) is a critical protein involved in the biosynthesis of the molybdenum cofactor (Moco), an essential component required for the activity of molybdenum-dependent enzymes, such as sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. These enzymes play vital roles in cellular metabolism, detoxification, and redox reactions. Moco deficiency, often caused by mutations in *MOCS2* or related genes, leads to severe neurological impairments and early mortality in humans, underscoring the protein's biological significance.
The *MOCS2* gene encodes a bifunctional protein with two domains: MOCS2A and MOCS2B. MOCS2A catalyzes the conversion of precursor Z to molybdopterin (MPT), while MOCS2B adenylates MPT to form the active Moco. Due to the complexity of Moco synthesis and its instability, recombinant MOCS2 protein production has become a key focus for studying Moco-related pathways and developing therapeutic strategies for Moco deficiency disorders.
Recombinant MOCS2 proteins are typically expressed in heterologous systems like *E. coli* or mammalian cell cultures, enabling scalable production for biochemical and structural studies. These proteins facilitate research into enzyme kinetics, protein-protein interactions, and the molecular mechanisms underlying Moco biosynthesis. Additionally, recombinant MOCS2 holds promise for enzyme replacement therapy or gene therapy to address congenital Moco deficiencies.
Recent advances in protein engineering and structural biology have enhanced the stability and functional characterization of MOCS2. providing insights into its dual enzymatic activities and regulatory roles. Its study also contributes to broader applications in biotechnology, such as optimizing molybdenum-dependent biocatalysts. Overall, MOCS2 recombinant protein serves as a vital tool for both basic research and translational medicine in metabolic and genetic disorders.
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