| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UGCGL2 |
| Uniprot No | Q9NYU1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-278 aa |
| 活性数据 | MAPAKATNVVRLLLGSTALWLSQLGSGTVAASKSVTAHLAAKWPETPLLLEASEFMAEESNEKFWQFLETVQELAIYKQTESDYSYYNLILKKAGQFLDNLHINLLKFAFSIRAYSPAIQMFQQIAADEPPPDGCNAFVVIHKKHTCKINEIKKLLKKAASRTRPYLFKGDHKFPTNKENLPVVILYAEMGTRTFSAFHKVLSEKAQNEEILYVLRHYIQKPSSRKMYLSGYGVELAIKSTEYKALDDTQVKTVTNTTVEDETETNEVQGFLFGKLKS |
| 分子量 | 56.32 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下是关于重组人UGCGL2蛋白的模拟参考文献示例(注：UGCGL2可能为特定研究中的命名，请结合实际情况验证名称准确性)：
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1. **文献名称**：*Production and Functional Analysis of Recombinant Human UGCGL2 in Glycolipid Synthesis*
**作者**：Chen L, et al.
**摘要**：本研究利用哺乳动物表达系统成功表达并纯化了重组人UGCGL2蛋白。功能实验表明，该蛋白在神经节苷脂生物合成中发挥关键作用，通过催化UDP-葡萄糖向神经酰胺的转移促进糖脂代谢。
2. **文献名称**：*Structural Insights into UGCGL2: A Novel Glycosyltransferase in Cancer Cell Membranes*
**作者**：Smith R, Patel K.
**摘要**：通过X射线晶体学解析了UGCGL2的三维结构，发现其具有独特的底物结合口袋。体外活性实验提示其过表达可能通过调节细胞膜糖脂组成影响肿瘤细胞侵袭能力。
3. **文献名称**：*UGCGL2 Knockdown Alters Lysosomal Glycolipid Storage in Human Fibroblasts*
**作者**：Yamamoto H, et al.
**摘要**：研究通过siRNA沉默UGCGL2基因，发现溶酶体内糖脂蓄积显著增加，提示UGCGL2在维持脂质稳态中的潜在作用，为相关代谢疾病机制提供新视角。
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**注**：以上内容为模拟生成的示例，实际研究中UGCGL2可能对应不同基因命名或研究主题。建议通过PubMed、Google Scholar等平台使用关键词(如"UGCGL2"、"recombinant protein")检索最新文献，或确认蛋白名称的正确性(例如是否为**UGCG**或**UGDH**等相关蛋白)。
Recombinant human UGCGL2 (UDP-glucose ceramide glucosyltransferase-like 2) protein is a genetically engineered form of a key enzyme involved in glycosphingolipid biosynthesis. UGCGL2. part of the glycosyltransferase 2 family, catalyzes the transfer of glucose from UDP-glucose to ceramide, forming glucosylceramide—a fundamental precursor for complex glycosphingolipids. These lipids are critical components of cell membranes, influencing signal transduction, cell adhesion, and membrane trafficking. The recombinant version is typically produced in heterologous systems (e.g., E. coli, mammalian cells) to ensure high purity and activity for experimental or therapeutic use. Studies suggest UGCGL2 dysregulation may link to lipid storage disorders, neurodegenerative diseases, and cancer progression, making it a target for drug discovery. Its recombinant expression enables structural analysis (e.g., X-ray crystallography) to elucidate substrate-binding mechanisms and design inhibitors. Additionally, it serves as a tool to explore glycosphingolipid roles in pathogen-host interactions, such as viral entry or bacterial toxin binding. Unlike endogenous UGCGL2. the recombinant protein often includes tags (His-tag, FLAG) for simplified purification and detection. Research gaps remain in understanding tissue-specific isoforms and post-translational modifications, highlighting the importance of recombinant models in advancing both basic and applied glycobiology.
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