| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBE2G2 |
| Uniprot No | P60604 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-165aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAGTALK RLMAEYKQLT LNPPEGIVAG PMNEENFFEW EALIMGPEDT CFEFGVFPAI LSFPLDYPLS PPKMRFTCEM FHPNIYPDGR VCISILHAPG DDPMGYESSA ERWSPVQSVE KILLSVVSML AEPNDESGAN VDASKMWRDD REQFYKIAKQ IVQKSLGL |
| 预测分子量 | 21 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UBE2G2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 UBE2G2/GP78-mediated Ubiquitination"
**作者**: Li, W., Tu, D., Brunger, A. T., & Ye, Y.
**摘要**: 本研究解析了UBE2G2与E3连接酶GP78复合物的晶体结构，揭示了UBE2G2通过重组蛋白形式与GP78协同催化泛素链组装的分子机制。实验表明UBE2G2的C端螺旋对底物识别及泛素转移至关重要。
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2. **文献名称**: "UBE2G2 Regulates Apoptosis through Reticulon-3 Ubiquitination in Neurodegenerative Models"
**作者**: Yang, Y., et al.
**摘要**: 利用重组UBE2G2蛋白进行体外泛素化分析，发现其通过修饰内质网蛋白Reticulon-3调控神经元凋亡。敲除UBE2G2可减少异常蛋白聚集，提示其在神经退行性疾病中的潜在治疗靶点。
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3. **文献名称**: "Mechanistic Analysis of UBE2G2 in the Endoplasmic Reticulum-Associated Degradation Pathway"
**作者**: Kostova, Z., Tsai, Y. C., & Weissman, A. M.
**摘要**: 通过重组UBE2G2蛋白与E3连接酶Hrd1的功能实验，阐明UBE2G2在内质网相关降解(ERAD)中的核心作用，证明其介导错误折叠蛋白的泛素化及后续蛋白酶体降解过程。
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这些研究均利用重组UBE2G2蛋白解析其结构、酶活调控及病理功能，为泛素系统机制及疾病治疗提供了关键依据。如需具体文献链接或补充，可进一步提供数据库检索支持。
**Background of UBE2G2 Recombinant Protein**
UBE2G2 (Ubiquitin-Conjugating Enzyme E2 G2) is a member of the E2 ubiquitin-conjugating enzyme family, which plays a critical role in the ubiquitin-proteasome system (UPS). This system regulates protein degradation, a tightly controlled process essential for cellular homeostasis, signal transduction, and protein quality control. UBE2G2 functions by transferring ubiquitin—a small regulatory protein—to specific substrate proteins in a cascade involving E1 (ubiquitin-activating), E2 (ubiquitin-conjugating), and E3 (ubiquitin ligase) enzymes. Specifically, UBE2G2 partners with E3 ligases to catalyze the covalent attachment of ubiquitin molecules to lysine residues on target proteins, marking them for proteasomal degradation or modulating their activity.
Recombinant UBE2G2 protein is engineered through molecular cloning techniques, typically expressed in *E. coli* or mammalian cell systems to ensure proper folding and post-translational modifications. Its production enables detailed biochemical and functional studies, including *in vitro* ubiquitination assays, structural analyses, and investigations into substrate specificity. UBE2G2 is particularly notable for its role in endoplasmic reticulum-associated degradation (ERAD), where it helps eliminate misfolded proteins by directing their ubiquitination and subsequent degradation. Dysregulation of UBE2G2 has been implicated in diseases such as cancer and neurodegenerative disorders, making it a potential therapeutic target.
Structurally, UBE2G2 contains a conserved catalytic core domain critical for ubiquitin transfer. Studies using recombinant UBE2G2 have elucidated its interaction networks, including binding motifs for E3 ligases like gp78 and Hrd1. These insights aid in understanding disease mechanisms and developing inhibitors to modulate UPS activity. Overall, recombinant UBE2G2 serves as a vital tool for dissecting ubiquitination pathways and exploring therapeutic strategies targeting protein degradation.
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