| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMA |
| Uniprot No | P78417 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-241aa |
| 氨基酸序列 | SGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL VLKAKGIRHE VININLKNKP EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMILELF SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW FERLEAMKLN ECVDHTPKLK LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG L |
| 预测分子量 | 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MMA(甲基丙二酸血症)重组蛋白研究的3篇示例文献，涵盖不同研究方向：
1. **文献名称**：*Recombinant human methylmalonyl-CoA mutase for enzyme replacement therapy in methylmalonic acidemia*
**作者**：Carrillo-Carrasco et al.
**摘要**：研究利用HEK293细胞表达重组人甲基丙二酰辅酶A变位酶(MUT)，通过体外实验和小鼠模型验证其酶活性和代谢纠正效果，为酶替代疗法提供实验依据。
2. **文献名称**：*Protein engineering of methylmalonyl-CoA mutase to enhance stability and activity*
**作者**：Wilkemeyer et al.
**摘要**：通过定点突变优化重组MUT酶的热稳定性和催化效率，在细菌表达系统中实现高产量纯化，并证明突变体在细胞模型中更有效降低甲基丙二酸水平。
3. **文献名称**：*Adeno-associated virus-mediated gene therapy for methylmalonic acidemia using engineered MUT variants*
**作者**：Chandler et al.
**摘要**：结合重组MUT蛋白与AAV载体递送，在小鼠模型中实现长期酶活性恢复，显著减少血液和尿液中毒性代谢物积累，探索基因-酶联合治疗策略。
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**提示**：若需真实文献，建议通过PubMed或Google Scholar搜索关键词“recombinant protein methylmalonic acidemia”或“MUT enzyme replacement therapy”获取最新研究。
**Background of MMA Recombinant Proteins**
Methylmalonic acidemia (MMA) is a rare inherited metabolic disorder caused by defects in enzymes involved in mitochondrial propionate metabolism, particularly methylmalonyl-CoA mutase (MCM) or its cofactor adenosylcobalamin (AdoCbl). This results in the accumulation of methylmalonic acid and toxic metabolites, leading to severe clinical manifestations such as metabolic acidosis, neurological impairment, and organ damage. Traditional therapeutic approaches, including dietary restrictions and vitamin supplementation, often show limited efficacy, necessitating novel strategies like enzyme replacement therapy (ERT) or gene therapy.
Recombinant protein technology has emerged as a promising avenue for addressing MMA. Recombinant proteins are engineered using genetic engineering to produce functional enzymes in heterologous systems (e.g., bacteria, yeast, or mammalian cells). For MMA, recombinant MCM or modified variants could potentially restore metabolic pathways by converting methylmalonyl-CoA to succinyl-CoA, reducing toxic buildup. Advances in protein engineering, such as codon optimization, post-translational modifications, and fusion tags, enhance the stability, solubility, and activity of these proteins.
Challenges remain, including ensuring efficient delivery of recombinant enzymes to mitochondria, overcoming immune responses, and achieving long-term efficacy. However, preclinical studies using recombinant MCM in cell and animal models have demonstrated reduced metabolite levels and improved survival rates. Additionally, recombinant proteins may serve as tools for studying MMA pathophysiology or screening therapeutic compounds.
The development of MMA recombinant proteins aligns with broader trends in precision medicine, aiming to provide tailored treatments for genetic disorders. Collaborations between academia and biotech companies are accelerating translational research, with clinical trials anticipated in the coming years. If successful, these therapies could transform the management of MMA, offering hope for patients with limited treatment options.
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