| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UGGT2 |
| Uniprot No | Q9NYU1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1516aa |
| 氨基酸序列 | MAPAKATNVVRLLLGSTALWLSQLGSGTVAASKSVTAHLAAKWPETPLLLEASEFMAEESNEKFWQFLETVQELAIYKQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQQIAADEPPPDGCNAFVVIHKKHTCKINEIKKLLKKAASRTRPYLFKGDHKFPTNKENLPVVILYAEMGTRTFSAFHKVLSEKAQNEEILYVLRHYIQKPSSRKMYLSGYGVELAIKSTEYKALDDTQVKTVTNTTVEDETETNEVQGFLFGKLKEIYSDLRDNLTAFQKYLIESNKQMMPLKVWELQDLSFQAASQIMSAPVYDSIKLMKDISQNFPIKARSLTRIAVNQHMREEIKENQKDLQVRFKIQPGDARLFINGLRVDMDVYDAFSILDMLKLEGKMMNGLRNLGINGEDMSKFLKLNSHIWEYTYVLDIRHSSIMWINDLENDDLYITWPTSCQKLLKPVFPGSVPSIRRNFHNLVLFIDPAQEYTLDFIKLADVFYSHEVPLRIGFVFILNTDDEVDGANDAGVALWRAFNYIAEEFDISEAFISIVHMYQKVKKDQNILTVDNVKSVLQNTFPHANIWDILGIHSKYDEERKAGASFYKMTGLGPLPQALYNGEPFKHEEMNIKELKMAVLQRMMDASVYLQREVFLGTLNDRTNAIDFLMDRNNVVPRINTLILRTNQQYLNLISTSVTADVEDFSTFFFLDSQDKSAVIAKNMYYLTQDDESIISAVTLWIIADFDKPSGRKLLFNALKHMKTSVHSRLGIIYNPTSKINEENTAISRGILAAFLTQKNMFLRSFLGQLAKEEIATAIYSGDKIKTFLIEGMDKNAFEKKYNTVGVNIFRTHQLFCQDVLKLRPGEMGIVSNGRFLGPLDEDFYAEDFYLLEKITFSNLGEKIKGIVENMGINANNMSDFIMKVDALMSSVPKRASRYDVTFLRENHSVIKTNPQENDMFFNVIAIVDPLTREAQKMAQLLVVLGKIINMKIKLFMNCRGRLSEAPLESFYRFVLEPELMSGANDVSSLGPVAKFLDIPESPLLILNMITPEGWLVETVHSNCDLDNIHLKDTEKTVTAEYELEYLLLEGQCFDKVTEQPPRGLQFTLGTKNKPAVVDTIVMAHHGYFQLKANPGAWILRLHQGKSEDIYQIVGHEGTDSQADLEDIIVVLNSFKSKILKVKVKKETDKIKEDILTDEDEKTKGLWDSIKSFTVSLHKENKKEKDVLNIFSVASGHLYERFLRIMMLSVLRNTKTPVKFWLLKNYLSPTFKEVIPHMAKEYGFRYELVQYRWPRWLRQQTERQRIIWGYKILFLDVLFPLAVDKIIFVDADQIVRHDLKELRDFDLDGAPYGYTPFCDSRREMDGYRFWKTGYWASHLLRRKYHISALYVVDLKKFRRIGAGDRLRSQYQALSQDPNSLSNLDQDLPNNMIYQVAIKSLPQDWLWCETWCDDESKQRAKTIDLCNNPKTKESKLKAAARIVPEWVEYDAEIRQLLDHLENKKQDTILTHDEL |
| 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UGGT2重组蛋白的3篇代表性文献及其摘要概括：
1. **文献名称**：*"Functional characterization of recombinant human UDP-glucose glycoprotein glucosyltransferase 2 (UGGT2) in endoplasmic reticulum quality control"*
**作者**：Sousa MC, et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了重组人UGGT2蛋白，证实其能够特异性识别未正确折叠的糖蛋白，并通过葡萄糖基化标记靶标蛋白，揭示了UGGT2在内质网质量控制中的关键作用。
2. **文献名称**：*"Structural insights into UGGT2-mediated substrate recognition through cryo-EM analysis"*
**作者**：Wang Y, et al.
**摘要**：通过冷冻电镜技术解析了重组UGGT2与底物复合物的结构，发现其通过两个独立结构域协同作用识别错误折叠的糖蛋白，为开发针对UGGT2相关疾病的调控策略提供了结构基础。
3. **文献名称**：*"Development of a high-throughput assay for UGGT2 enzymatic activity using recombinant protein"*
**作者**：Tanaka K, et al.
**摘要**：利用昆虫细胞表达系统制备活性重组UGGT2.并建立荧光标记的高通量酶活检测方法，证实该方法可用于筛选UGGT2抑制剂，为研究内质网相关代谢疾病提供工具。
注：以上文献信息为示例性内容，实际文献需通过PubMed或Web of Science检索确认。建议使用关键词"UGGT2 recombinant"+"expression/function/structure"查询最新研究。
UGGT2 (UDP-glucose:glycoprotein glucosyltransferase 2) is a key enzyme involved in the quality control of glycoprotein folding within the endoplasmic reticulum (ER). As a member of the UGGT family, it acts as a folding sensor by selectively recognizing misfolded or incompletely folded glycoproteins. UGGT2 catalyzes the transfer of glucose from UDP-glucose to N-linked glycans on target proteins, effectively "tagging" them for re-entry into the calnexin/calreticulin folding cycle. This glucosylation process ensures that proteins achieve proper tertiary structure before exiting the ER, playing a critical role in maintaining proteostasis.
Structurally, UGGT2 contains a catalytic domain and a lectin-like domain that enables substrate recognition. While UGGT1. its paralog, is ubiquitously expressed, UGGT2 shows tissue-specific prevalence, with higher activity in the liver and certain secretory cells. Both enzymes share overlapping functions but may exhibit substrate preferences, though their distinct biological roles remain under investigation.
Recombinant UGGT2 is typically produced using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications and functional activity. The purified protein is valuable for studying ER quality control mechanisms, particularly in diseases like cancer, neurodegenerative disorders, and congenital disorders of glycosylation where protein misfolding is implicated. Researchers utilize recombinant UGGT2 to reconstitute glucosylation assays, investigate substrate specificity, and develop potential modulators of ER stress pathways. Its application extends to biopharmaceutical quality control, where understanding glycoprotein folding is crucial for therapeutic protein production. Recent studies also explore UGGT2's potential as a biomarker or therapeutic target for conditions involving chronic ER stress.
×
