| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AGA |
| Uniprot No | P20933 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-346aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSSSPLPLVVNTWPFKNATEAAWRALASG GSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVG AVGDLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTA SQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGILKQDIPIHKETED DRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDT AGAAAATGNGDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFPEF FGAVICANVTGSYGAACNKLSTFTQFSFMVYNSEKNQPTEEKVDCI |
| 预测分子量 | 37 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AGA(天冬氨酸氨基葡萄糖苷酶)重组蛋白的模拟参考文献示例，涵盖不同研究方向：
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1. **标题**：*Expression and Characterization of Recombinant Human Aspartylglucosaminidase in HEK293 Cells*
**作者**：Smith J, et al.
**期刊**：*Journal of Biological Chemistry* (2018)
**摘要**：本研究利用HEK293哺乳动物表达系统成功表达了具有生物活性的重组AGA蛋白，并通过亲和层析纯化。酶活性分析表明，重组AGA可有效水解合成荧光底物，为酶替代疗法研究奠定基础。
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2. **标题**：*Structural Analysis of Recombinant AGA Using Cryo-EM: Implications for Lysosomal Storage Disorders*
**作者**：Chen L, et al.
**期刊**：*Nature Structural & Molecular Biology* (2020)
**摘要**：通过冷冻电镜解析了重组AGA的三维结构，揭示了其催化活性位点和突变相关疾病(如天冬氨酰葡萄糖胺尿症)的分子机制，为靶向药物设计提供结构依据。
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3. **标题**：*High-Yield Production of Recombinant AGA in Pichia pastoris and Therapeutic Efficacy in a Mouse Model*
**作者**：Müller R, et al.
**期刊**：*Biotechnology and Bioengineering* (2019)
**摘要**：在毕赤酵母中优化了AGA重组表达，产量达50 mg/L。动物实验显示，纯化蛋白可显著改善模型小鼠的溶酶体贮积症状，支持其作为潜在治疗药物的开发。
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**备注**：以上文献为示例性质，实际研究中建议通过PubMed或Web of Science检索关键词(如“recombinant AGA protein”、“aspartylglucosaminidase expression”)获取最新实证数据。
**Background of Recombinant AGA Protein**
Recombinant AGA (α-galactosidase A) protein is a genetically engineered enzyme designed to address deficiencies in individuals with Fabry disease, a rare X-linked lysosomal storage disorder. Fabry disease arises from mutations in the *GLA* gene, leading to reduced or absent activity of α-galactosidase A, an enzyme responsible for breaking down globotriaosylceramide (Gb3) and other glycolipids. Accumulation of these substrates in lysosomes results in progressive multi-organ damage, affecting the kidneys, heart, and nervous system.
The development of recombinant AGA leverages recombinant DNA technology, where the human *GLA* gene is expressed in cultured host cells, typically Chinese hamster ovary (CHO) cells. This process ensures large-scale production of the functional enzyme, which is purified and formulated for therapeutic use. Two prominent examples are agalsidase alfa (Replagal) and agalsidase beta (Fabrazyme), both approved for enzyme replacement therapy (ERT). These recombinant proteins are administered intravenously, enabling cellular uptake via mannose-6-phosphate receptors to restore lysosomal function.
Research on recombinant AGA has expanded beyond ERT, exploring advanced strategies like gene therapy and mRNA-based treatments to improve efficacy and accessibility. Additionally, recombinant AGA serves as a critical tool in biochemical research, aiding in the study of enzyme kinetics, substrate specificity, and disease mechanisms. Despite challenges, including immune responses and high costs, recombinant AGA remains a cornerstone in managing Fabry disease, highlighting the transformative potential of biotechnology in treating genetic disorders.
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