| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GBA1 |
| Uniprot No | P04062 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 40-536aa |
| 氨基酸序列 | ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ |
| 预测分子量 | 61.2 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. |
1. **"Production of Recombinant Human β-Glucocerebrosidase in Chinese Hamster Ovary Cells"**
- *作者：Aerts JM et al.*
- **摘要**：该研究描述了在CHO细胞中高效表达重组人GBA1酶的方法，验证了其酶活性及糖基化修饰对溶酶体靶向性的影响，为戈谢病替代疗法提供生产基础。
2. **"Pharmacokinetic and Pharmacodynamic Properties of Recombinant Glucocerebrosidase in Gaucher Disease Patients"**
- *作者：Grabowski GA et al.*
- **摘要**：通过临床试验评估重组GBA1蛋白(伊米苷酶)在戈谢病患者中的药代动力学，证实其可显著降低底物积累并改善肝脾肿大等临床症状。
3. **"Stabilization of Recombinant GBA1 by Chaperone Molecules for Enhanced Enzyme Delivery"**
- *作者：Yang C et al.*
- **摘要**：研究利用小分子伴侣(如ambroxol)结合重组GBA1蛋白，提高其热稳定性及穿越血脑屏障的能力，探索其在神经型戈谢病及帕金森病中的潜在应用。
4. **"A Novel Plant-Based Expression System for Recombinant Human Glucocerebrosidase"**
- *作者：Shaditel Y et al.*
- **摘要**：开发基于植物细胞(烟草)的重组GBA1生产平台，证明其与哺乳动物系统产物具有可比活性，且成本更低，为大规模生产提供替代方案。
**Background of GBA1 Recombinant Protein**
GBA1. encoding the enzyme glucocerebrosidase (GCase), is a critical gene involved in glycosphingolipid metabolism. GCase hydrolyzes glucocerebroside into glucose and ceramide within lysosomes, maintaining cellular lipid homeostasis. Mutations in *GBA1* are linked to Gaucher disease (GD), a lysosomal storage disorder characterized by GCase deficiency, leading to toxic accumulations of glucocerebroside in macrophages and visceral organs. Notably, *GBA1* variants are also the most common genetic risk factor for Parkinson’s disease (PD), implicating lysosomal dysfunction in neurodegenerative mechanisms.
Recombinant GCase proteins, produced via genetic engineering, are therapeutic tools for GD. The first FDA-approved enzyme replacement therapy (ERT), alglucerase (1994), was later replaced by imiglucerase, a recombinant human GCase produced in Chinese hamster ovary (CHO) cells. Other variants, like velaglucerase alfa (human cell line-derived) and taliglucerase alfa (plant cell-based), offer alternatives with improved efficacy or reduced immunogenicity.
Beyond ERT, recombinant GBA1 proteins are explored for PD and related synucleinopathies. Preclinical studies suggest enhancing GCase activity may reduce α-synuclein aggregation, a hallmark of PD. Challenges remain in optimizing delivery, stability, and blood-brain barrier penetration. Novel approaches include PEGylation to prolong half-life, chaperone molecules to stabilize mutant GCase, and gene therapies to enable endogenous production.
Research continues to refine recombinant GBA1 platforms, including yeast or insect cell systems, and structure-guided engineering to enhance catalytic efficiency. These efforts aim to address unmet needs in GD, expand therapeutic potential for neurodegenerative diseases, and deepen understanding of GCase biology.
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