| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBE2G1 |
| Uniprot No | P62253 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-170aa |
| 氨基酸序列 | MTELQSALLL RRQLAELNKN PVEGFSAGLI DDNDLYRWEV LIIGPPDTLY EGGVFKAHLT FPKDYPLRPP KMKFITEIWH PNVDKNGDVC ISILHEPGED KYGYEKPEER WLPIHTVETI MISVISMLAD PNGDSPANVD AAKEWREDRN GEFKRKVARC VRKSQETAFE |
| 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UBE2G1重组蛋白的虚构参考文献示例(仅供格式参考，非真实文献)：
1. **文献名称**：Structural Insights into UBE2G1 Recombinant Protein in Ubiquitin Transfer Mechanism
**作者**：Chen L, et al.
**摘要**：本研究通过X射线晶体学解析了UBE2G1重组蛋白的三维结构，揭示了其与E3连接酶RNF123的相互作用界面，阐明了UBE2G1在泛素转移过程中的构象变化机制。
2. **文献名称**：UBE2G1-Mediated Protein Degradation in Breast Cancer Cell Lines
**作者**：Wang Y, et al.
**摘要**：通过体外重组UBE2G1蛋白实验，发现其过度表达可促进雌激素受体α(ERα)的泛素化降解，抑制乳腺癌细胞增殖，提示UBE2G1作为潜在治疗靶点的价值。
3. **文献名称**：Functional Characterization of Recombinant UBE2G1 in Parkinson's Disease Models
**作者**：Smith J, et al.
**摘要**：利用重组UBE2G1蛋白研究其在α-突触核蛋白清除中的作用，发现UBE2G1通过增强错误折叠蛋白的泛素化标记，减缓神经元退行性病变进程。
4. **文献名称**：UBE2G1 Recombinant Protein Interaction Screening via Yeast Two-Hybrid System
**作者**：Tanaka K, et al.
**摘要**：采用重组UBE2G1蛋白进行酵母双杂交筛选，鉴定出新型底物蛋白P53的新泛素化调控通路，为癌症治疗提供新方向。
注：以上文献信息为模拟内容，实际引用请通过PubMed或Google Scholar检索真实文献。
UBE2G1 (Ubiquitin-Conjugating Enzyme E2 G1) is a member of the E2 ubiquitin-conjugating enzyme family, which plays a critical role in the ubiquitin-proteasome system (UPS) by mediating the transfer of ubiquitin to substrate proteins. As an E2 enzyme, UBE2G1 works in tandem with E3 ubiquitin ligases to catalyze the covalent attachment of ubiquitin molecules to lysine residues on target proteins. This post-translational modification typically marks proteins for proteasomal degradation, though it can also regulate cellular processes like DNA repair, signal transduction, and endoplasmic reticulum-associated degradation (ERAD).
The recombinant UBE2G1 protein is engineered for in vitro studies to dissect its biochemical functions, substrate specificity, and interaction networks. Structurally, it contains a conserved catalytic core domain (UBC fold) required for ubiquitin binding and thioester bond formation. Researchers often utilize recombinant UBE2G1 to investigate its role in forming K48-linked polyubiquitin chains, a canonical signal for proteasomal targeting. Studies have linked UBE2G1 dysregulation to diseases such as cancer and neurodegenerative disorders, highlighting its therapeutic relevance.
Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), recombinant UBE2G1 is purified with affinity tags (e.g., His-tag) for functional assays. Its applications span enzymology, structural studies (e.g., crystallography), and high-throughput drug screening to identify UPS modulators. Ongoing research aims to clarify its isoform-specific functions and regulatory mechanisms in cellular homeostasis, offering insights into UPS-targeted therapies.
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