| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GH1 |
| Uniprot No | P01241 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-217aa |
| 氨基酸序列 | FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF |
| 预测分子量 | 27.1 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GH1重组蛋白的3篇示例文献摘要，内容为虚构，仅供参考：
1. **标题**: "Efficient Expression and Purification of Recombinant Human GH1 in Escherichia coli"
**作者**: Zhang L, Wang Y, Chen H
**摘要**: 研究报道了通过优化大肠杆菌表达系统实现人GH1蛋白的高效可溶性表达，采用亲和层析纯化获得高纯度产物，并验证其生物活性。
2. **标题**: "Structural Characterization of Recombinant GH1 Produced in Pichia pastoris"
**作者**: Smith J, Brown K, Lee S
**摘要**: 利用毕赤酵母真核表达系统制备GH1蛋白，通过X射线晶体学解析其三维结构，揭示了翻译后修饰对其受体结合能力的影响。
3. **标题**: "Functional Analysis of Mutant GH1 Recombinant Proteins in Growth Disorders"
**作者**: Gupta R, Tanaka M, Rossi F
**摘要**: 构建了多种GH1突变体重组蛋白，通过体外细胞实验评估其促生长功能缺陷，为生长激素缺乏症的分子机制提供新见解。
注：以上文献信息为模拟内容，实际引用请查询真实数据库。
GH1 recombinant protein, derived from the glycoside hydrolase family 1 (GH1), is a class of enzymes critical in breaking down glycosidic bonds in carbohydrates, particularly β-linked oligo- and polysaccharides. These enzymes are widely distributed in nature, playing essential roles in metabolic processes such as cellulose degradation, plant defense mechanisms, and lactose metabolism. The GH1 family includes β-glucosidases, β-galactosidases, and other substrate-specific enzymes, which are pivotal in bioenergy production, food processing, and pharmaceutical applications.
Recombinant GH1 proteins are engineered using genetic cloning and heterologous expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to achieve high purity, scalability, and functional consistency. This approach allows researchers to study enzyme kinetics, substrate specificity, and structure-function relationships without interference from native cellular components. GH1 enzymes often feature a conserved (β/α)₈ TIM barrel fold, with catalytic residues (glutamate or aspartate) enabling acid/base-assisted hydrolysis.
In biotechnology, GH1 recombinant proteins are utilized in biofuel production to hydrolyze cellulose into fermentable sugars, enhancing lignocellulosic biomass conversion. In medicine, they serve as therapeutic agents for genetic disorders like Gaucher’s disease, where β-glucosidase deficiency leads to lysosomal storage complications. Additionally, GH1 enzymes are explored for lactose-free dairy processing and synthetic biology applications.
Recent advances focus on engineering thermostable or pH-tolerant GH1 variants via directed evolution or computational design, addressing industrial process limitations. Despite progress, challenges remain in optimizing expression yields, reducing production costs, and improving catalytic efficiency for diverse substrates. Ongoing research aims to unlock GH1’s full potential in sustainable industries and precision medicine.
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