| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMAB |
| Uniprot No | Q96EY8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-250 aa |
| 活性数据 | QSRGPQGV EDGDRPQPSS KTPRIPKIYT KTGDKGFSST FTGERRPKDD QVFEAVGTTD ELSSAIGFAL ELVTEKGHTF AEELQKIQCT LQDVGSALAT PCSSAREAHL KYTTFKAGPI LELEQWIDKY TSQLPPLTAF ILPSGGKISS ALHFCRAVCR RAERRVVPLV QMGETDANVA KFLNRLSDYL FTLARYAAMK EGNQEKIYMK NDPSAESEGL |
| 分子量 | 27.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人MMAB蛋白的3篇文献摘要示例(注：以下内容为基于主题的模拟示例，具体文献需检索数据库核实)：
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1. **文献名称**: *Expression and functional characterization of recombinant human MMAB protein in Escherichia coli*
**作者**: Zhang Y, et al.
**摘要**: 本研究利用大肠杆菌系统成功表达并纯化了重组人MMAB蛋白，证实其催化钴胺素(维生素B12)转化为腺苷钴胺素(AdoCbl)的活性，并通过酶动力学分析揭示了关键突变对功能的影响。
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2. **文献名称**: *Structural insights into MMAB-mediated ATP:Co(I)rrinoid adenosyltransferase mechanism*
**作者**: Padovani D, Banerjee R.
**摘要**: 通过X射线晶体学解析了重组人MMAB蛋白的三维结构，揭示了其依赖ATP的钴胺素腺苷转移机制，为甲基丙二酸尿症cblB型的致病突变提供了分子层面的解释。
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3. **文献名称**: *Defective MMAB disrupts mitochondrial metabolism and induces oxidative stress in patient-derived cell models*
**作者**: Chandler RJ, et al.
**摘要**: 研究利用重组MMAB蛋白修复患者来源的细胞模型，证明MMAB功能缺失导致线粒体丙酸代谢异常和活性氧积累，强调了其在能量代谢中的关键作用。
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如需获取具体文献，建议通过PubMed或Google Scholar检索关键词：**recombinant MMAB protein**、**MMAB gene expression**、**methylmalonic aciduria cblB type**。
**Background of Recombinant Human MMAB Protein**
The human MMAB protein, encoded by the *MMAB* gene, is a mitochondrial enzyme critical in vitamin B12 (cobalamin) metabolism. It functions as an adenosyltransferase, catalyzing the conversion of inactive vitamin B12 into its active adenosylcobalamin (AdoCbl) form. This cofactor is essential for methylmalonyl-CoA mutase (MCM), an enzyme that converts methylmalonyl-CoA to succinyl-CoA during the breakdown of branched-chain amino acids, odd-chain fatty acids, and cholesterol. Defects in MMAB disrupt this pathway, leading to methylmalonic acidemia (MMA), an inherited metabolic disorder characterized by toxic accumulation of methylmalonic acid and life-threatening complications.
Recombinant human MMAB protein is produced via genetic engineering, enabling studies on its structure, enzymatic mechanisms, and interactions within the mitochondrial matrix. Research focuses on understanding its role in cobalamin processing, substrate binding, and regulatory motifs influencing activity. Recombinant MMAB also holds therapeutic potential, as enzyme replacement or gene therapies could address MMA caused by *MMAB* mutations. Additionally, it serves as a tool for drug screening, biomarker development, and elucidating molecular pathways linking vitamin B12 deficiency to metabolic dysfunction. By bridging molecular biology and clinical insights, recombinant MMAB remains pivotal in advancing diagnostics and targeted treatments for metabolic diseases.
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