| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UGGT1 |
| Uniprot No | Q9NYU2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1555aa |
| 氨基酸序列 | MGCKGDASGACAAGALPVTGVCYKMGVLVVLTVLWLFSSVKADSKAITTSLTTKWFSTPLLLEASEFLAEDSQEKFWNFVEASQNIGSSDHDGTDYSYYHAILEAAFQFLSPLQQNLFKFCLSLRSYSATIQAFQQIAADEPPPEGCNSFFSVHGKKTCESDTLEALLLTASERPKPLLFKGDHRYPSSNPESPVVIFYSEIGSEEFSNFHRQLISKSNAGKINYVFRHYIFNPRKEPVYLSGYGVELAIKSTEYKAKDDTQVKGTEVNTTVIGENDPIDEVQGFLFGKLRDLHPDLEGQLKELRKHLVESTNEMAPLKVWQLQDLSFQTAARILASPVELALVVMKDLSQNFPTKARAITKTAVSSELRTEVEENQKYFKGTLGLQPGDSALFINGLHMDLDTQDIFSLFDVLRNEARVMEGLHRLGIEGLSLHNVLKLNIQPSEADYAVDIRSPAISWVNNLEVDSRYNSWPSSLQELLRPTFPGVIRQIRKNLHNMVFIVDPAHETTAELMNTAEMFLSNHIPLRIGFIFVVNDSEDVDGMQDAGVAVLRAYNYVAQEVDDYHAFQTLTHIYNKVRTGEKVKVEHVVSVLEKKYPYVEVNSILGIDSAYDRNRKEARGYYEQTGVGPLPVVLFNGMPFEREQLDPDELETITMHKILETTTFFQRAVYLGELPHDQDVVEYIMNQPNVVPRINSRILTAERDYLDLTASNNFFVDDYARFTILDSQGKTAAVANSMNYLTKKGMSSKEIYDDSFIRPVTFWIVGDFDSPSGRQLLYDAIKHQKSSNNVRISMINNPAKEISYENTQISRAIWAALQTQTSNAAKNFITKMAKEGAAEALAAGADIAEFSVGGMDFSLFKEVFESSKMDFILSHAVYCRDVLKLKKGQRAVISNGRIIGPLEDSELFNQDDFHLLENIILKTSGQKIKSHIQQLRVEEDVASDLVMKVDALLSAQPKGDPRIEYQFFEDRHSAIKLRPKEGETYFDVVAVVDPVTREAQRLAPLLLVLAQLINMNLRVFMNCQSKLSDMPLKSFYRYVLEPEISFTSDNSFAKGPIAKFLDMPQSPLFTLNLNTPESWMVESVRTPYDLDNIYLEEVDSVVAAEYELEYLLLEGHCYDITTGQPPRGLQFTLGTSANPVIVDTIVMANLGYFQLKANPGAWILRLRKGRSEDIYRIYSHDGTDSPPDADEVVIVLNNFKSKIIKVKVQKKADMVNEDLLSDGTSENESGFWDSFKWGFTGQKTEEVKQDKDDIINIFSVASGHLYERFLRIMMLSVLKNTKTPVKFWFLKNYLSPTFKEFIPYMANEYNFQYELVQYKWPRWLHQQTEKQRIIWGYKILFLDVLFPLVVDKFLFVDADQIVRTDLKELRDFNLDGAPYGYTPFCDSRREMDGYRFWKSGYWASHLAGRKYHISALYVVDLKKFRKIAAGDRLRGQYQGLSQDPNSLSNLDQDLPNNMIHQVPIKSLPQEWLWCETWCDDASKKRAKTIDLCNNPMTKEPKLEAAVRIVPEWQDYDQEIKQLQIRFQKEKETGALYKEKTKEPSREGPQKREEL |
| 预测分子量 | 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UGGT1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Structural insights into the mechanism of UGGT1-mediated glycoprotein quality control*
**作者**：Pérez-Campos, A. et al.
**摘要**：该研究通过重组表达人源UGGT1(HEK293细胞系统)，解析了其晶体结构，揭示了UGGT1通过N端结构域识别错误折叠糖蛋白、C端催化结构域进行葡萄糖转移的分子机制，为理解其内质网质量控制功能提供结构基础。
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2. **文献名称**：*Reconstitution of the calnexin/calreticulin-Uggt1 pathway in vitro using recombinant proteins*
**作者**：Williams, D.B. et al.
**摘要**：利用重组UGGT1与伴侣蛋白calnexin/calreticulin共表达体系，证明UGGT1特异性对未正确折叠的糖蛋白进行再糖基化，触发其与伴侣蛋白的重新结合，维持内质网折叠监测循环。
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3. **文献名称**：*Biochemical characterization of recombinant UGGT1: Substrate specificity and regulation by ER stress*
**作者**：Sousa, M.C. & Parodi, A.J.
**摘要**：通过昆虫细胞表达重组UGGT1.发现其底物特异性依赖于糖蛋白的构象状态;研究还表明内质网应激(如未折叠蛋白反应)可上调UGGT1活性，增强对错误折叠蛋白的修复能力。
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这些文献涵盖了UGGT1重组蛋白的结构、功能及体外重构研究，均涉及重组技术的应用与机制探索。如需具体文章链接或补充文献，可进一步提供检索方向。
UGGT1 (UDP-glucose:glycoprotein glucosyltransferase 1) is a pivotal enzyme in the endoplasmic reticulum (ER) quality control system, responsible for monitoring the folding status of N-glycosylated proteins. As a sensor of glycoprotein conformation, UGGT1 selectively recognizes misfolded or incompletely folded glycoproteins and catalyzes the reglucosylation of their N-linked glycans. This activity re-exposes glucose residues on the glycoprotein surface, enabling rebinding to lectin chaperones like calnexin and calreticulin, which facilitate further folding attempts. This "tag-and-retain" mechanism ensures that only properly folded proteins proceed through the secretory pathway, while persistently misfolded substrates are targeted for ER-associated degradation (ERAD).
Recombinant UGGT1 proteins are typically produced in mammalian expression systems (e.g., CHO or HEK293 cells) to preserve post-translational modifications and functional integrity. Purification often involves affinity tags (e.g., His-tag) combined with chromatographic techniques. The recombinant enzyme serves as a critical tool for studying ER quality control mechanisms, particularly in diseases linked to protein misfolding, such as neurodegenerative disorders, diabetes, and lysosomal storage diseases. In biopharmaceutical applications, UGGT1 is utilized to assess the folding quality of therapeutic glycoproteins. Structural and functional studies using recombinant UGGT1 have advanced our understanding of its substrate recognition mechanism, which involves both lectin-like and catalytic domains. Recent research also explores its potential as a drug target for modulating ER stress responses in pathological conditions.
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