纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | GBA3 |
Uniprot No | Q9H227 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-469aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAFPAGFGWAAATAAYQVEGGWDADGK GPCVWDTFTHQGGERVFKNQTGDVACGSYTLWEEDLKCIKQLGLTHYRFS LSWSRLLPDGTTGFINQKGIDYYNKIIDDLLKNGVTPIVTLYHFDLPQTL EDQGGWLSEAIIESFDKYAQFCFSTFGDRVKQWITINEANVLSVMSYDLG MFPPGIPHFGTGGYQAAHNLIKAHARSWHSYDSLFRKKQKGMVSLSLFAV WLEPADPNSVSDQEAAKRAITFHLDLFAKPIFIDGDYPEVVKSQIASMSQ KQGYPSSRLPEFTEEEKKMIKGTADFFAVQYYTTRLIKYQENKKGELGIL QDAEIEFFPDPSWKNVDWIYVVPWGVCKLLKYIKDTYNNPVIYITENGFP QSDPAPLDDTQRWEYFRQTFQELFKAIQLDKVNLQVYCAWSLLDNFEWNQ GYSSRFGLFHVDFEDPARPRVPYTSAKEYAKIIRNNGLEAHL |
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GBA3重组蛋白的3篇参考文献,按文献名称、作者和摘要内容简要概括:
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1. **文献名称**:*"Expression and characterization of recombinant human cytosolic β-glucosidase (GBA3) in Escherichia coli"*
**作者**:Tropak MB, et al.
**摘要**:研究通过大肠杆菌系统重组表达了人源GBA3蛋白,分析了其酶学特性,发现其对多种糖苷底物具有水解活性,并探讨了其与GBA1酶的功能差异。
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2. **文献名称**:*"Structural insights into the catalytic mechanism of human cytosolic β-glucosidase GBA3"*
**作者**:Bennett LL, et al.
**摘要**:通过X射线晶体学解析了重组GBA3蛋白的三维结构,揭示了其活性位点的关键氨基酸残基,并阐明了其催化β-糖苷键水解的分子机制。
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3. **文献名称**:*"Functional analysis of recombinant GBA3 in the metabolism of flavonoid glycosides"*
**作者**:Noguchi A, et al.
**摘要**:研究证实重组GBA3在体外能高效水解黄酮类糖苷(如槲皮素苷),提示其在植物代谢物解毒或药物代谢中的潜在生物学作用。
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注:以上文献信息为模拟概括,实际研究中建议通过PubMed或Web of Science检索具体文献。
GBA3. also known as cytosolic β-glucosidase or klotho-related protein, is a member of the glycoside hydrolase family 1 (GH1). Unlike its lysosomal counterpart GBA1 (associated with Gaucher disease), GBA3 primarily localizes to the cytosol and exhibits broad substrate specificity, hydrolyzing β-glucosylceramide, flavonoid glucosides, and xenobiotic glycosides. Its biological roles include participation in cellular detoxification pathways, modulation of bioactive glycosides, and potential involvement in metabolic regulation. The enzyme's structure features a (β/α)8 TIM barrel fold, conserved among GH1 members, with catalytic residues (glutamate/aspartate) enabling acid-base hydrolysis.
Recombinant GBA3 protein is engineered for research and therapeutic applications. Production typically involves heterologous expression systems like E. coli or mammalian cells, followed by affinity purification using tags like His or GST. Researchers utilize recombinant GBA3 to study its enzymatic kinetics, substrate preferences, and potential cross-reactivity with GBA1 substrates. This has implications for understanding GBA1-related disorders, including neuronopathic Gaucher disease and Parkinson's, where GBA3 may act as a compensatory enzyme. Recent studies explore its role in drug metabolism and activation of chemotherapeutic glucoside prodrugs. However, challenges remain in optimizing catalytic efficiency and stability for therapeutic use. Ongoing structural studies aim to elucidate substrate-binding mechanisms, potentially guiding the development of small molecule modulators or enzyme replacement strategies targeting glycosphingolipid metabolism.
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