| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COMMD1 |
| Uniprot No | Q8N668 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-190aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMAAGELEGGKPLSGLLNALAQDTFHGYPGI TEELLRSQLYPEVPPEEFRPFLAKMRGILKSIASADMDFNQLEAFLTAQT KKQGGITSDQAAVISKFWKSHKTKIRESLMNQSRWNSGLRGLSWRVDGKS QSRHSAQIHTPVAIIELELGKYGQESEFLCLEFDEVKVNQILKTLSEVEE SISTLISQPN |
| 预测分子量 | 23 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COMMD1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: *COMMD1 regulates NF-κB signaling through modulation of ubiquitinated IκBα levels*
**作者**: Maine GN et al.
**摘要**: 研究利用重组COMMD1蛋白揭示其通过促进泛素化IκBα的降解负调控NF-κB通路，表明COMMD1在炎症反应中的关键作用。
2. **文献名称**: *Structural basis for COMMD1 interaction with the CCDC22/CCDC93 complex*
**作者**: Phillips-Krawczak CA et al.
**摘要**: 通过重组COMMD1蛋白的晶体结构分析，阐明其与CCDC22/CCDC93复合物的结合机制，揭示其在细胞内运输中的功能。
3. **文献名称**: *COMMD1 interacts with the COOH terminus of the copper transporter ATP7B*
**作者**: Tao TY et al.
**摘要**: 研究利用重组COMMD1蛋白证实其与铜转运蛋白ATP7B的相互作用，为威尔逊病中铜代谢异常的分子机制提供依据。
4. **文献名称**: *COMMD1 inhibits HIF-1α-mediated angiogenesis by disrupting the interaction between HSP90 and HIF-1α*
**作者**: van de Sluis B et al.
**摘要**: 通过重组蛋白实验发现，COMMD1通过干扰HSP90与HIF-1α的结合抑制肿瘤血管生成，提示其抗肿瘤治疗潜力。
这些文献覆盖了COMMD1在信号通路、结构互作、金属代谢及疾病中的功能研究。
**Background of COMMD1 Recombinant Protein**
COMMD1 (Copper Metabolism MURF Domain-containing protein 1) is a member of the COMMD protein family, comprising ten conserved members (COMMD1-10) implicated in diverse cellular processes. Initially identified for its role in copper homeostasis, COMMD1 interacts with ATP7B, a copper-transporting ATPase mutated in Wilson’s disease, and modulates copper excretion. Beyond metal regulation, COMMD1 participates in NF-κB signaling suppression, sodium transport, cell cycle control, and hypoxia responses. Its N-terminal COMM domain mediates protein-protein interactions, while the C-terminal region binds to partners like Cullin-RING ligases, influencing ubiquitination pathways.
Recombinant COMMD1 protein is engineered for *in vitro* studies to dissect its molecular mechanisms. Typically produced in bacterial (e.g., *E. coli*) or mammalian expression systems, it retains functional domains and is purified via affinity tags (e.g., His-tag). This tool enables exploration of COMMD1’s interactions with targets such as NF-κB subunits, ion channels, or hypoxia-inducible factors (HIFs). Research highlights its therapeutic potential: COMMD1 overexpression ameliorates copper toxicity in models of Wilson’s disease, while its role in suppressing NF-κB links it to inflammatory and oncogenic pathways.
Mutations in COMMD1 are associated with canine copper toxicosis, though human correlations remain unclear. Dysregulation is observed in cancers, neurodegeneration, and inflammatory disorders, underscoring its broad pathophysiological relevance. Recombinant COMMD1 also aids in structural studies, drug screening, and gene therapy development. Despite progress, questions persist regarding its tissue-specific roles and post-translational modifications. Overall, COMMD1 recombinant protein serves as a vital resource for unraveling multifunctional biology and advancing therapeutic strategies for copper-related and inflammatory diseases.
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