| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C14orf143 |
| Uniprot No | Q9BUY7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-163 aa |
| 氨基酸序列 | MFFSEARARSRTWEASPSEHRKWVEVFKACDEDHKGYLSREDFKTAVVMLFGYKPSKIEVDSVMSSINPNTSGILLEGFLNIVRKKKEAQRYRNEVRHIFTAFDTYYRGFLTLEDFKKAFRQVAPKLPERTVLEVFREVDRDSDGHVSFRDFEYALNYGQKEA |
| 分子量 | 45.6 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 冻干粉 |
| 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. |
以下为3-4条关于重组人C14orf143蛋白的模拟参考文献(注：因文献可能不存在，建议通过PubMed等平台验证)：
1. **《C14orf143 Promotes Hepatocellular Carcinoma Proliferation by Regulating Cell Cycle》**
- 作者：Zhang L, et al.
- 摘要：研究发现C14orf143蛋白在肝癌组织中高表达，通过激活CDK2/cyclin E复合体调控细胞周期，促进肿瘤细胞增殖。
2. **《Structural and Functional Characterization of the Recombinant C14orf143 Protein》**
- 作者：Wang Y, et al.
- 摘要：首次报道重组人C14orf143蛋白的体外表达与纯化，结合晶体结构解析揭示其潜在核酸结合活性，提示其在DNA修复中的功能。
3. **《C14orf143 Interacts with Mitochondrial Proteins and Modulates Oxidative Stress Response》**
- 作者：Kim S, et al.
- 摘要：通过蛋白质互作组学分析，发现C14orf143与线粒体电子传递链蛋白结合，可能通过调节ROS水平影响细胞氧化应激应答。
4. **《C14orf143 Knockout Mice Exhibit Impaired Lipid Metabolism》**
- 作者：Müller R, et al.
- 摘要：基因敲除小鼠模型显示，C14orf143缺失导致肝脏脂质代谢紊乱，暗示其在脂肪酸氧化通路中的潜在作用。
**提示**：以上为模拟文献，具体研究需查阅真实数据库(如PubMed、Google Scholar)并验证C14orf143的最新命名(部分数据库可能已更新其基因符号，如TDRKH或其它)。
C14orf143. also known as MIDAS-containing protein (MIDEAS), is a human protein encoded by the C14orf143 gene located on chromosome 14q24.3. Although initially categorized as a poorly characterized open reading frame, recent studies have linked it to transcriptional regulation and chromatin remodeling processes. Structurally, MIDEAS contains a conserved MIDAS (metal ion-dependent adhesion site) motif, typically involved in protein-protein or protein-metal interactions, which suggests its potential role in macromolecular complex assembly.
Functionally, MIDEAS has been identified as a component of the SIN3A histone deacetylase (HDAC) complex, which mediates transcriptional repression by deacetylating histones and compacting chromatin. Research indicates that MIDEAS may act as a scaffold protein, stabilizing interactions between SIN3A and other corepressors, thereby modulating gene silencing. Its expression appears critical during cellular differentiation and development, with knockdown experiments showing disrupted cell cycle progression and altered expression of differentiation markers.
Dysregulation of MIDEAS has been implicated in diseases, particularly cancer. For instance, reduced MIDEAS expression correlates with poor prognosis in gliomas and breast cancers, possibly due to impaired transcriptional control of oncogenic pathways. Recombinant C14orf143 protein has been utilized in vitro to study its biochemical properties and interaction networks, facilitating insights into its role in epigenetic regulation. Further research is needed to elucidate its precise molecular mechanisms and therapeutic potential.
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