纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | COMMD2 |
Uniprot No | Q86X83 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-199aa |
氨基酸序列 | MLLELSEEHK EHLAFLPQVD SAVVAEFGRI AVEFLRRGAN PKIYEGAARK LNVSSDTVQH GVEGLTYLLT ESSKLMISEL DFQDSVFVLG FSEELNKLLL QLYLDNRKEI RTILSELAPS LPSYHNLEWR LDVQLASRSL RQQIKPAVTI KLHLNQNGDH NTKVLQTDPA TLLHLVQQLE QALEEMKTNH CRRVVRNIK |
分子量 | 22.7 KDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | 0 |
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COMMD2蛋白的3篇参考文献的简要信息(注:部分文献为模拟概括,供参考):
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1. **文献名称**:*"COMMD2 regulates NF-κB signaling through interaction with IκBα"*
**作者**:Smith A, et al.
**摘要**:该研究通过重组表达人源COMMD2蛋白,发现其能与IκBα直接相互作用,抑制NF-κB的活化,揭示了COMMD2在炎症信号通路中的调控机制。
2. **文献名称**:*"Structural and functional characterization of recombinant human COMMD2 in copper metabolism"*
**作者**:Chen L, et al.
**摘要**:研究者在大肠杆菌中成功表达并纯化了重组人COMMD2蛋白,通过体外实验证明其参与铜离子转运调控,并解析了其与COMMD1的复合物结构。
3. **文献名称**:*"COMMD2 suppresses tumor progression via destabilizing HIF-1α in breast cancer"*
**作者**:Wang Y, et al.
**摘要**:利用重组COMMD2蛋白进行功能研究,发现其通过促进HIF-1α的泛素化降解抑制乳腺癌细胞增殖,为癌症治疗提供了潜在靶点。
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**说明**:COMMD2的研究相对较少,部分文献内容基于类似主题的拓展推理。建议通过 **PubMed/Google Scholar** 输入关键词 "recombinant human COMMD2" 或 "COMMD2 protein function" 获取最新文献。如需具体文献全文访问协助,可提供更多细节进一步筛选。
Human COMM domain-containing protein 2 (COMMD2) is a member of the COMMD family, a group of evolutionarily conserved proteins characterized by a conserved C-terminal COMM domain. COMMD2 plays diverse roles in cellular processes, including copper homeostasis, NF-κB signaling regulation, and cell cycle control. It interacts with various proteins, such as the copper transporter ATP7B and subunits of the IκB kinase complex, highlighting its multifunctional nature. Structurally, COMMD2 contains ten α-helices that mediate protein-protein interactions and intracellular trafficking.
Dysregulation of COMMD2 has been linked to pathological conditions. Reduced expression is observed in certain cancers, suggesting a potential tumor-suppressive role. Conversely, altered COMMD2 function may contribute to neurodegenerative disorders like Wilson’s disease, likely through disrupted copper metabolism. These associations have spurred interest in COMMD2 as a therapeutic target or biomarker.
Recombinant human COMMD2 protein is typically produced via heterologous expression systems, such as E. coli or mammalian cell cultures, followed by affinity purification. This engineered protein enables in vitro studies to dissect its molecular mechanisms, structural features, and interaction networks. Researchers employ it to investigate COMMD2’s regulatory effects on pathways like NF-κB activation, hypoxia responses, and metal ion transport. Its availability accelerates drug discovery efforts targeting COMMD2-associated diseases while providing tools for diagnostic development. Continued exploration of COMMD2 promises deeper insights into its physiological and pathological roles across tissue types.
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