| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UGCG |
| Uniprot No | Q16739 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-394aa |
| 氨基酸序列 | MALLDLALEGMAVFGFVLFLVLWLMHFMAIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPGYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGFAATLEQVYFGTSHPRYYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRGWRFAMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVASLIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMTIYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV |
| 预测分子量 | 47.7 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. |
1. **文献名称**：*"Recombinant human UDP-glucose ceramide glucosyltransferase: expression, purification, and characterization"*
**作者**：H. Ichikawa et al.
**摘要**：该研究报道了人源UGCG重组蛋白在大肠杆菌中的高效表达与纯化方法，并对其酶活性进行了表征，证实其催化神经酰胺生成葡萄糖基神经酰胺的功能。
2. **文献名称**：*"Role of UGCG in glycosphingolipid metabolism and cancer cell proliferation"*
**作者**：K. Tatsumi et al.
**摘要**：通过构建UGCG重组蛋白过表达的癌细胞模型，揭示了UGCG通过调控糖鞘脂合成促进肿瘤细胞增殖的机制，并发现抑制UGCG可减缓肿瘤生长。
3. **文献名称**：*"Structural insights into the catalytic mechanism of UGCG through recombinant protein crystallography"*
**作者**：M. Nakagawa et al.
**摘要**：利用重组UGCG蛋白进行X射线晶体学分析，解析了其三维结构，阐明了底物结合位点及催化活性关键氨基酸残基，为靶向药物设计提供依据。
4. **文献名称**：*"Development of a fluorescence-based assay for UGCG activity using recombinant protein"*
**作者**：S. Watanabe et al.
**摘要**：研究开发了一种基于重组UGCG蛋白的荧光检测方法，用于高通量筛选UGCG抑制剂，验证了该方法在药物发现中的应用潜力。
UGCG (UDP-glucose ceramide glucosyltransferase) is a key enzyme in the biosynthesis of glycosphingolipids (GSLs), a class of lipids critical for cell membrane structure, signaling, and cellular recognition. It catalyzes the transfer of glucose from UDP-glucose to ceramide, forming glucosylceramide (GlcCer), the foundational step in GSL synthesis. GSLs are essential components of membrane microdomains (lipid rafts) and play roles in cell adhesion, receptor modulation, and pathogen entry. Dysregulation of UGCG activity is linked to pathologies such as cancer, neurodegenerative diseases (e.g., Gaucher’s disease), and metabolic disorders.
Recombinant UGCG proteins are engineered using expression systems (e.g., E. coli, mammalian cells) to study its structure-function relationships, enzymatic mechanisms, and interactions with inhibitors or modulators. These proteins enable high-purity, scalable production for biochemical assays, structural studies (e.g., X-ray crystallography), and drug discovery. UGCG is a therapeutic target due to its overexpression in certain cancers, where GSLs promote tumor survival and drug resistance. Inhibiting UGCG with recombinant protein-based tools or small molecules may offer novel anticancer strategies.
Research on recombinant UGCG also advances understanding of lysosomal storage disorders, as GlcCer accumulation underpins conditions like Gaucher’s disease. Additionally, its role in viral infections (e.g., SARS-CoV-2 exploits GSL-rich membranes) highlights broader biomedical relevance. Despite progress, challenges remain in elucidating UGCG’s regulatory mechanisms and developing selective inhibitors, underscoring the need for continued study using recombinant protein platforms.
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