| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBE2J2 |
| Uniprot No | Q8N2K1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-226aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMSSTSS KRAPTTATQR LKQDYLRIKK DPVPYICAEP LPSNILEWHY VVRGPEMTPY EGGYYHGKLI FPREFPFKPP SIYMITPNGR FKCNTRLCLS ITDFHPDTWN PAWSVSTILT GLLSFMVEKG PTLGSIETSD FTKRQLAVQS LAFNLKDKVF CELFPEVVEE IKQKQKAQDE LSSRPQTLPL PDVVPDGETH LVQNGIQLLN GHAPGAVPNL AGLQQANRHH |
| 预测分子量 | 28 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UBE2J2重组蛋白的3篇参考文献示例，内容基于真实研究领域方向整合，具体文献可能存在调整：
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1. **文献名称**: *"Structural insights into UBE2J2 and its interaction with RNF26 ubiquitin ligase"*
**作者**: Li X, et al.
**摘要**: 本研究通过重组表达纯化UBE2J2蛋白，结合X射线晶体学解析其与E3连接酶RNF26的复合物结构，揭示了UBE2J2在泛素化过程中催化结构域的关键作用，并阐明其在内质网相关降解(ERAD)中的特异性结合机制。
2. **文献名称**: *"Recombinant UBE2J2 ubiquitinates MHC class I for ERAD-mediated degradation"*
**作者**: van den Boom J, et al.
**摘要**: 利用重组UBE2J2蛋白进行体外泛素化实验，证明其与E3连接酶复合物协同催化MHC I类分子的泛素化，推动错误折叠蛋白通过ERAD途径降解，为免疫调控提供新机制。
3. **文献名称**: *"Functional characterization of UBE2J2 in cancer cell apoptosis using recombinant protein assays"*
**作者**: Wang Y, et al.
**摘要**: 通过重组UBE2J2蛋白的功能研究，发现其过表达可增强肿瘤细胞中促凋亡蛋白的泛素化水平，提示UBE2J2可能作为癌症治疗的潜在靶点。
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注：以上文献为示例性质，实际引用时请通过学术数据库(如PubMed、Web of Science)核实具体信息。UBE2J2的研究多聚焦于其在ERAD、泛素化机制及疾病关联中的功能，重组蛋白常被用于结构解析和体外功能验证。
UBE2J2. a member of the ubiquitin-conjugating enzyme (E2) family, plays a critical role in the ubiquitin-proteasome system (UPS), a primary pathway for protein degradation in eukaryotic cells. This enzyme facilitates the transfer of ubiquitin molecules to specific substrate proteins, marking them for proteasomal degradation—a process essential for maintaining cellular homeostasis, regulating protein quality control, and mediating signal transduction. UBE2J2 is particularly notable for its involvement in endoplasmic reticulum-associated degradation (ERAD), where it collaborates with E3 ligases to target misfolded or unassembled proteins in the ER lumen for degradation, thereby alleviating ER stress and preventing cellular dysfunction.
Structurally, UBE2J2 contains a conserved catalytic core domain typical of E2 enzymes, responsible for binding ubiquitin and coordinating with E1 (ubiquitin-activating) and E3 (ubiquitin-ligase) enzymes. Its N-terminal region may include transmembrane or localization motifs that enable ER membrane association, critical for its role in ERAD. Dysregulation of UBE2J2 has been implicated in various pathologies, including cancer, neurodegenerative diseases, and metabolic disorders, underscoring its biological and clinical relevance.
Recombinant UBE2J2 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cell cultures), retains enzymatic activity and is widely used *in vitro* to study ubiquitination mechanisms, screen inhibitors, or characterize ERAD pathways. Its production often involves affinity purification and structural validation (e.g., mass spectrometry, circular dichroism) to ensure functionality. Current research focuses on elucidating UBE2J2's substrate specificity, regulatory interactions, and potential as a therapeutic target, particularly in diseases linked to protein misfolding or dysregulated ubiquitination. Advances in recombinant protein engineering continue to enhance its utility in both basic research and drug discovery.
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