| 纯度 | >95%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | UDP |
| Uniprot No | P12758 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-253aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSKSDVFHLGLTKNDLQGATLAIVPGDPDR VEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEE LAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPA VADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERYDTYSGRVVRHF KGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPN AETMKQTESHAVKIVVEAARRLL |
| 预测分子量 | 29 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UDP(尿苷二磷酸)与重组蛋白相关研究的示例性参考文献(注：部分文献为示例性质，非真实存在，仅供格式参考)：
1. **文献名称**：*Metabolic Engineering of UDP-Sugar Pools in CHO Cells for Enhanced Glycosylation of Recombinant Proteins*
**作者**：Smith J. et al.
**摘要**：研究通过代谢工程手段调控CHO细胞中UDP-糖(如UDP-葡萄糖、UDP-半乳糖)的供应，优化重组蛋白(如抗体)的糖基化修饰，提高其稳定性和治疗效果。
2. **文献名称**：*In Vitro Glycosylation of Recombinant Proteins Using UDP-GlcNAc and Bacterial Glycosyltransferases*
**作者**：Chen L. et al.
**摘要**：利用UDP-N-乙酰葡萄糖胺(UDP-GlcNAc)和工程化糖基转移酶，在体外对重组蛋白进行定点糖基化修饰，拓展其在生物制药中的应用潜力。
3. **文献名称**：*UDP-Glucose Pyrophosphorylase Overexpression Enhances Recombinant Protein Production in E. coli*
**作者**：Wang Y. et al.
**摘要**：通过在大肠杆菌中过表达UDP-葡萄糖焦磷酸化酶，提高UDP-葡萄糖的胞内水平，促进重组蛋白的糖基化前体合成，显著提升产量。
4. **文献名称**：*Role of UDP-Glc in Protein Quality Control during Recombinant Expression in Yeast*
**作者**：Kim S. et al.
**摘要**：探究酿酒酵母中UDP-葡萄糖对重组蛋白折叠的调控作用，发现其通过内质网应激通路减少蛋白聚集，提高分泌效率。
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**说明**：以上文献为示例，实际研究中需通过PubMed、Web of Science等数据库检索真实文献。关键词建议：**UDP-sugar metabolism**, **recombinant protein glycosylation**, **metabolic engineering**, **in vitro enzymatic modification**。
**Background of UDP-Recombinant Proteins**
UDP-recombinant proteins are engineered biomolecules designed to study or manipulate processes involving uridine diphosphate (UDP)-dependent enzymes, such as glycosyltransferases, glucuronosyltransferases, or synthases. These enzymes play critical roles in metabolic pathways, including carbohydrate metabolism, post-translational modifications, and detoxification. For instance, UDP-glucuronosyltransferases (UGTs) catalyze the conjugation of UDP-glucuronic acid to drugs or toxins, enhancing their solubility for excretion.
Recombinant protein technology enables the production of these enzymes in heterologous systems (e.g., *E. coli*, yeast, or mammalian cells*) for research and industrial applications. By expressing UDP-dependent enzymes recombinantly, scientists overcome challenges in isolating them from native tissues, such as low abundance or instability. This approach also allows for protein engineering to improve catalytic efficiency, substrate specificity, or stability under industrial conditions.
UDP-recombinant proteins are pivotal in drug development, particularly in studying drug metabolism and toxicity. They facilitate high-throughput screening of enzyme inhibitors or substrates, aiding in personalized medicine. Additionally, they are used in synthesizing glycoconjugates (e.g., vaccines, biologics) through enzymatic glycosylation, offering advantages over chemical methods in precision and scalability.
Challenges include maintaining proper folding and post-translational modifications in simpler hosts, which may affect activity. Advances in expression systems, structural biology, and directed evolution continue to address these limitations. Overall, UDP-recombinant proteins bridge fundamental research and biotechnological applications, driving innovations in therapeutics, biocatalysis, and synthetic biology.
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