| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GFUS |
| Uniprot No | Q13630 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-321aa |
| 氨基酸序列 | MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEKVQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPDKTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNFNIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPIILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTPFKQAVKETCAWFTDNYEQARK |
| 预测分子量 | 40.0 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GFUS(GDP-L-岩藻糖合成酶)重组蛋白的3篇参考文献概览：
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1. **文献名称**: *Expression and characterization of recombinant human GDP-L-fucose synthase in Escherichia coli*
**作者**: Smith A, et al.
**摘要**: 研究报道了人源GFUS在大肠杆菌中的高效重组表达及纯化方法，分析了其酶动力学特性，验证了其在岩藻糖代谢中的功能，为糖基化工程提供基础数据。
2. **文献名称**: *Structural insights into the catalytic mechanism of GDP-L-fucose synthase*
**作者**: Zhang Y, et al.
**摘要**: 通过X射线晶体学解析了重组GFUS的三维结构，揭示了其底物结合位点和催化机制，为设计岩藻糖代谢相关疾病的抑制剂提供了结构基础。
3. **文献名称**: *Functional analysis of GFUS in inflammatory bowel disease using a recombinant protein model*
**作者**: Lee H, et al.
**摘要**: 利用重组GFUS蛋白研究其在肠道炎症模型中的作用，发现其通过调控岩藻糖基化修饰影响免疫细胞黏附，提示其作为潜在治疗靶点。
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注：以上文献信息为示例性概括，实际文献需通过学术数据库(如PubMed、Web of Science)检索确认。如需具体文献，建议结合研究主题补充关键词(如"recombinant expression"或"enzyme kinetics")进一步筛选。
**Background of GFUS Recombinant Protein**
The GFUS recombinant protein is a genetically engineered biomolecule designed to facilitate advanced research and therapeutic applications. Derived from the fusion of specific functional domains, GFUS typically integrates a target protein of interest with a stabilizing or affinity tag, such as glutathione-S-transferase (GST) or polyhistidine (His-tag), to enhance expression, purification, or detection. This protein is synthesized using recombinant DNA technology, where the coding sequence of the target gene is cloned into an expression vector and transfected into host cells, such as *E. coli*, yeast, or mammalian cell lines. The choice of host depends on the complexity of the protein’s post-translational modifications required for functionality.
GFUS recombinant proteins are pivotal in structural and functional studies, enabling researchers to investigate protein-protein interactions, enzymatic activities, and cellular signaling pathways. Their high purity and specificity, achieved through affinity chromatography and other purification techniques, make them valuable tools in drug discovery, vaccine development, and diagnostic assays. Additionally, GFUS variants may be engineered to include mutations or modifications to study disease-related mechanisms or optimize therapeutic efficacy.
In therapeutic contexts, recombinant proteins like GFUS have revolutionized biologics, offering targeted treatments for cancers, autoimmune disorders, and infectious diseases. Their scalability and reproducibility in production align with industrial standards, ensuring consistent quality for clinical use. Ongoing advancements in protein engineering, such as site-specific conjugation or fusion with half-life extenders (e.g., Fc regions), further expand their biomedical potential. Overall, GFUS recombinant proteins exemplify the synergy between molecular biology and biotechnology, driving innovations across research and healthcare.
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