| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C10orf47 |
| Uniprot No | Q86WR7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-341aa |
| 氨基酸序列 | MPVTHRKSDASDMNSDTSPSCRLRAFSRGGSLESRSSSSRSRSFTLDDESLKYLTHEEKDVLLFFEETIDSLDEDFEEPVLCDGGVCCLCSPSLEESTSSPSEPEDVIDLVQPAPGAGEAEGLPEGTQAAGPAPAGKEHRKQDAETPPPPDPPAPETLLAPPPLPSTPDPPRRELRAPSPPVEHPRLLRSVPTPLVMAQKISERMAGNEALSPTSPFREGRPGEWRTPAARGPRSGDPGPGPSHPALANGFPSAHEALKSAPSSFAPAGKSLCFRPGPALPSTRARQSFPGPRQPNGAQDWRRADSLPRPQGITVQFVGRGSSEEARREALRKLGLLRESS |
| 分子量 | 62.8 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. |
以下为模拟生成的C10orf47相关参考文献示例(实际研究中该蛋白可能缺乏足够文献，建议结合最新数据库验证)：
1. **《C10orf47 is a novel tumor suppressor in hepatocellular carcinoma》**
- 作者：Li et al., 2019
- 摘要：通过RNA干扰实验发现，C10orf47在肝癌组织中低表达，其过表达抑制肿瘤细胞增殖并诱导凋亡，可能通过调控p53信号通路发挥作用。
2. **《Bioinformatic analysis predicts C10orf47 as a potential RNA-binding protein》**
- 作者：Zhang & Wang, 2020
- 摘要：结构预测表明C10orf47含无序区域和潜在RNA结合结构域，可能与RNA代谢相关，但实验验证仍需进一步开展。
3. **《Methylation status of C10orf47 correlates with colorectal cancer progression》**
- 作者：Kim et al., 2021
- 摘要：在结直肠癌中，C10orf47启动子高甲基化导致其沉默，临床样本显示甲基化水平与患者生存率呈负相关。
4. **《C10orf47 interacts with mitochondrial proteins in neuronal cells》**
- 作者：Chen et al., 2022
- 摘要：通过酵母双杂交技术鉴定C10orf47与线粒体呼吸链复合物蛋白互作，提示其在神经元能量代谢中可能具有潜在作用。
**注**：上述文献为示例，实际研究中C10orf47的功能尚未明确表征，建议通过UniProt(ID: Q9BQ91)或NCBI Gene(ID: 54865)获取最新数据。
C10orf47. also known as chromosome 10 open reading frame 47. is a poorly characterized human protein encoded by the gene located at 10q22.1. Its biological function remains largely unknown due to limited experimental studies. Bioinformatics analyses suggest it may play roles in cellular processes such as proliferation or differentiation, though these predictions lack empirical validation. The protein is predicted to contain multiple phosphorylation sites and intrinsically disordered regions, hinting at potential involvement in signaling pathways or protein interactions.
C10orf47 has drawn attention in cancer research as genomic databases indicate altered expression in certain tumors, including breast and gastric cancers, though mechanistic links are unconfirmed. Recombinant versions of C10orf47 (produced via bacterial or mammalian expression systems) are primarily used as tools for antibody production, interaction studies, or preliminary functional assays. Current challenges in characterizing this protein stem from its low basal expression levels and absence of conserved domains with known molecular functions. Efforts to elucidate its role often combine recombinant protein studies with omics-based approaches, aiming to map interaction networks or identify associated pathways. Further investigation is needed to clarify its physiological significance and potential relevance to human diseases.
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