纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | UgDH |
Uniprot No | O60701 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-494aa |
氨基酸序列 | MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSELEMFEIKKICCIG AGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVV ESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEA CARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPE FLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTT NTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRI GNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQR RRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEG AHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAV VICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIET IGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV |
预测分子量 | 60 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UgDH(UDP-glucose dehydrogenase)重组蛋白研究的示例性参考文献(注:以下内容为示例,具体文献需根据实际检索结果调整):
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1. **标题**: *Heterologous expression and characterization of recombinant UDP-glucose dehydrogenase from *Bacillus subtilis***
**作者**: Smith J, et al.
**摘要**: 研究在大肠杆菌中成功表达并纯化了来源于枯草芽孢杆菌的UgDH重组蛋白,分析了其最适pH、温度及金属离子对酶活性的影响,为糖胺聚糖合成途径优化提供基础。
2. **标题**: *Crystallographic analysis of UDP-glucose dehydrogenase reveals substrate-binding mechanism*
**作者**: Lee S, et al.
**摘要**: 通过X射线晶体学解析了重组UgDH的三维结构,揭示了其与底物UDP-glucose的结合模式,阐明了催化过程中关键氨基酸残基的作用机制。
3. **标题**: *Engineering recombinant UgDH for enhanced hyaluronic acid production in *E. coli***
**作者**: Zhang Y, et al.
**摘要**: 通过定向进化技术改造UgDH,提高了其催化效率,并将其应用于工程菌株中,显著提升了透明质酸的产量,展示了其在生物制造中的应用潜力。
4. **标题**: *Comparative study of UgDH expression in prokaryotic and eukaryotic systems*
**作者**: Gupta R, et al.
**摘要**: 对比分析了大肠杆菌和毕赤酵母系统表达UgDH的差异,发现酵母系统表达的酶具有更高稳定性,为工业化生产提供了系统选择依据。
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建议通过PubMed、Web of Science等平台以**“UDP-glucose dehydrogenase recombinant”**或**“UgDH expression”**为关键词检索最新文献以获取具体信息。
**Background of UgDH Recombinant Protein**
UgDH (UDP-glucose dehydrogenase) is a key enzyme involved in the synthesis of glycosaminoglycans (GAGs) and bacterial polysaccharides, catalyzing the NAD+-dependent oxidation of UDP-glucose to UDP-glucuronic acid. This reaction is critical for producing precursors essential for extracellular matrix components like hyaluronic acid, heparin, and chondroitin sulfate, which play roles in cell signaling, tissue development, and pathogenicity.
Recombinant UgDH proteins are engineered via heterologous expression systems (e.g., *E. coli*, yeast) to study its structure-function relationships, enzymatic mechanisms, and regulatory roles. The enzyme’s tetrameric structure, cofactor binding sites, and substrate specificity have been explored to optimize industrial applications, including biopolymer production and metabolic engineering. UgDH is also studied in pathogenic bacteria (e.g., *Streptococcus pneumoniae*) for its role in synthesizing capsular polysaccharides, which are virulence factors, making it a potential antimicrobial target.
In biotechnology, recombinant UgDH enables scalable production of UDP-glucuronic acid, a precursor for synthesizing bioactive molecules. Its applications extend to biomedical research, such as modulating GAG-related pathways in cancer, fibrosis, and inflammation. Recent studies focus on engineering thermostable or high-activity UgDH variants to enhance industrial efficiency. Challenges include maintaining protein solubility and stability during expression.
Overall, UgDH recombinant protein serves as a vital tool in both basic research and applied sciences, bridging enzymology, synthetic biology, and therapeutic development.
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