| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GBA |
| Uniprot No | P04062-1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 40-536aa |
| 氨基酸序列 | ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRME LSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPA QNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLP EEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQ PGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLG FTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPE AAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQ SVRLGSWDRGMQYSHSIITSLLYHVVGWTDWNLALNPEGGPNWVRNFVDS PIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALM HPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ |
| 预测分子量 | 56 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GBA(葡萄糖脑苷脂酶)重组蛋白研究的3篇示例文献(注：文献为虚构示例，实际引用需检索数据库)：
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1. **文献名称**：Production of Recombinant Human Glucocerebrosidase in Plant Cell Cultures
**作者**：Zhang Y, et al.
**摘要**：本研究开发了一种基于植物细胞培养体系(如烟草细胞)高效表达重组人GBA蛋白的方法，通过基因优化和糖基化修饰，显著提高了蛋白的酶活性和稳定性，为戈谢病治疗提供了新型药物开发策略。
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2. **文献名称**：Structural Analysis of Recombinant GBA1 for Substrate Binding Optimization
**作者**：Smith J, et al.
**摘要**：通过X射线晶体学解析了重组GBA蛋白的三维结构，揭示了其底物结合口袋的关键氨基酸残基，并利用定点突变技术改良了酶对脂质底物的催化效率，为治疗神经退行性疾病(如帕金森病)提供理论依据。
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3. **文献名称**：Pharmacokinetic Evaluation of Recombinant GBA in Gaucher Disease Model Mice
**作者**：Lee H, et al.
**摘要**：在戈谢病小鼠模型中评估了重组GBA蛋白(imiglucerase类似物)的药代动力学特性，证实其通过静脉注射后能有效降低肝脾中葡萄糖脑苷脂蓄积，并验证了其长期治疗的安全性和剂量依赖性效应。
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如需真实文献，建议检索PubMed或Web of Science，关键词：**"recombinant glucocerebrosidase" "production" "GBA1" "Gaucher disease"**。实际经典研究可参考制药公司(如Genzyme/Sanofi)开发的伊米苷酶(imiglucerase)相关文献。
**Background of Recombinant GBA Protein**
The glucocerebrosidase (GBA) enzyme, encoded by the *GBA1* gene, plays a critical role in lysosomal metabolism by breaking down glucocerebroside into glucose and ceramide. Deficiencies in GBA activity lead to Gaucher disease, a lysosomal storage disorder characterized by the accumulation of glucocerebroside in macrophages, resulting in organ damage, bone abnormalities, and neurological symptoms in severe cases. Historically, treatment relied on enzyme replacement therapy (ERT) using purified human placental GBA, but limited supply and immunological challenges prompted the development of recombinant GBA proteins.
Recombinant GBA is produced via genetic engineering, typically using mammalian cell systems (e.g., Chinese hamster ovary (CHO) cells) to ensure proper post-translational modifications, such as glycosylation, critical for enzyme stability and lysosomal targeting. The first FDA-approved recombinant GBA, imiglucerase (1990s), marked a breakthrough in Gaucher disease management, offering scalable production and reduced immunogenicity. Subsequent iterations, including velaglucerase alfa (produced in human fibroblast cells) and taliglucerase alfa (plant-cell-based expression), further diversified production platforms and improved patient access.
Beyond Gaucher disease, recombinant GBA has garnered interest in Parkinson’s disease research, as *GBA1* mutations are a common genetic risk factor. Preclinical studies explore its potential to mitigate alpha-synuclein aggregation and neurotoxicity. However, challenges persist, including high production costs, short half-life, and limited blood-brain barrier penetration. Innovations like PEGylation, engineered variants with enhanced stability, and gene therapy approaches aim to address these limitations. Overall, recombinant GBA remains a cornerstone of precision medicine for lysosomal disorders, with ongoing research expanding its therapeutic scope.
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