| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MGAM |
| Uniprot No | O43451 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 87-954aa |
| 氨基酸序列 | SAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEW |
| 预测分子量 | 101.1 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MGAM(麦芽糖-葡萄糖淀粉酶，Maltase-Glucoamylase)重组蛋白的模拟参考文献示例，供参考：
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1. **文献名称**: *Expression and Characterization of Recombinant Human Maltase-Glucoamylase for Therapeutic Applications*
**作者**: Zhang, L., et al.
**摘要**: 本研究成功在HEK293细胞中表达了功能性重组人MGAM蛋白，并优化了其纯化工艺。实验表明，重组MGAM具有与天然酶相似的催化活性，可水解α-1.4-糖苷键，为开发糖尿病治疗药物提供了基础。
2. **文献名称**: *Structural Insights into the Catalytic Mechanism of MGAM through Site-Directed Mutagenesis*
**作者**: Kumar, S., & Lee, J. H.
**摘要**: 通过定点突变和晶体结构分析，揭示了MGAM的N端和C端结构域在底物特异性中的差异，阐明了其水解淀粉类物质的分子机制，为设计特异性抑制剂提供结构依据。
3. **文献名称**: *Development of MGAM-Specific Inhibitors Using Recombinant Enzyme Screening*
**作者**: Rossi, M., et al.
**摘要**: 利用重组MGAM蛋白进行高通量筛选，发现两种小分子化合物可显著抑制MGAM活性，可能通过延缓碳水化合物消化降低餐后血糖，具有抗糖尿病潜力。
4. **文献名称**: *Comparative Analysis of MGAM Expression in Prokaryotic vs. Eukaryotic Systems*
**作者**: Chen, X., & Wang, Y.
**摘要**: 对比大肠杆菌和昆虫杆状病毒系统表达MGAM的效果，发现真核系统表达的蛋白具有更优的折叠和酶活性，强调了表达系统选择对重组酶功能研究的重要性。
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**注意**：以上文献信息为模拟内容，实际研究中请通过PubMed、Web of Science或Google Scholar等平台检索验证。建议结合关键词“recombinant MGAM”、“Maltase-Glucoamylase expression”或“MGAM inhibitors”获取真实文献。
**Background of MGAM Recombinant Protein**
Maltase-glucoamylase (MGAM), a critical enzyme in starch digestion, belongs to the α-glucosidase family and is primarily expressed in the intestinal brush border. It catalyzes the hydrolysis of α-1.4-glycosidic bonds in oligosaccharides into glucose, playing a key role in carbohydrate metabolism and postprandial glucose regulation. MGAM consists of two catalytic subunits: the N-terminal subunit (MGAM-N) and the C-terminal subunit (MGAM-C), each with distinct substrate preferences and kinetic properties. Dysregulation of MGAM activity is linked to metabolic disorders, including diabetes and obesity, making it a therapeutic target.
Recombinant MGAM proteins are engineered using heterologous expression systems (e.g., bacterial, yeast, or mammalian cells) to produce purified, functional enzymes for research and drug development. These proteins retain the enzymatic activity and structural features of native MGAM, enabling studies on substrate specificity, inhibitor screening, and mechanistic investigations. For instance, MGAM inhibitors like acarbose are used to slow glucose absorption in diabetes management.
The development of MGAM recombinant proteins has advanced understanding of starch metabolism and supported the design of targeted therapies. Their applications extend to diagnostic tools, enzyme replacement strategies, and personalized medicine. Additionally, structural studies using recombinant MGAM have elucidated active-site architectures, facilitating rational drug design.
Overall, MGAM recombinant proteins serve as vital tools in both basic research and translational medicine, bridging insights into carbohydrate biology and therapeutic innovation.
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