| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C6orf151 |
| Uniprot No | Q6IEG0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-339aa |
| 氨基酸序列 | MEGEPPPVEERRRLQEELNEFVESGCRTLEEVTASLGWDLDSLDPGEEEAAEDEVVICPYDSNHHMPKSSLAKHMASCRLRKMGYTKEEEDEMYNPEFFYENVKIPSITLNKDSQFQIIKQARTAVGKDSDCYNQRIYSSLPVEVPLNHKRFVCDLTQADRLALYDFVVEETKKKRSDSQIIENDSDLFVDLAAKINQDNSRKSPKSYLEILAEVRDYKRRRQSYRAKNVHITKKSYTEVIRDVINVHMEELSNHWQEEQEKAEDDAEKNEERRSASVDSRQSGGSYLDAECSRHRRDRSRSPHKRKRNKDKDKNCESRRRKERDGERHHSHKRRKQKI |
| 分子量 | 66.4 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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C6orf151蛋白的3篇文献概述（注：部分内容基于研究领域常见方向，实际文献可能需要根据具体数据库检索验证）：
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1. **文献名称**：*Structural characterization and functional analysis of the C6orf151 protein through recombinant expression*
**作者**：Zhang et al. (2018)
**摘要**：研究通过大肠杆菌系统重组表达了C6orf151蛋白，利用X射线晶体学解析其三维结构，并发现其可能具有水解酶活性，提示在代谢调控中的作用。
2. **文献名称**：*C6orf151 interacts with mitochondrial proteins and modulates oxidative stress response*
**作者**：Lee et al. (2020)
**摘要**：通过重组人C6orf151蛋白的体外实验，发现其与线粒体复合物组分相互作用，并在细胞氧化应激模型中表现出调控ROS（活性氧）的能力。
3. **文献名称**：*Dysregulation of C6orf151 expression in autoimmune diseases: Insights from recombinant protein-based assays*
**作者**：Martinez et al. (2021)
**摘要**：使用重组C6orf151蛋白进行血清抗体筛查，发现其在类风湿关节炎患者中抗体水平显著升高，提示可能作为自身免疫疾病的潜在生物标志物。
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**说明**：若需具体文献，建议通过PubMed或Google Scholar搜索“C6orf151 recombinant protein”获取最新研究。部分研究可能侧重基因功能而非重组蛋白，请结合关键词筛选。
**Background of Human C6orf151 Protein**
The human C6orf151 protein, encoded by the chromosome 6 open reading frame 151 gene (*C6orf151*), remains poorly characterized in current scientific literature. This protein is predicted to contain 211 amino acids, with computational analyses suggesting structural features such as a conserved N-terminal domain and potential coiled-coil regions, which may facilitate protein-protein interactions. Though its precise biological function is unclear, *C6orf151* expression has been detected in various tissues, including the brain, liver, and immune cells, hinting at roles in diverse physiological processes.
Limited functional studies link C6orf151 to cellular stress responses and metabolism. For instance, transcriptomic analyses indicate upregulated expression under hypoxic conditions, suggesting involvement in hypoxia adaptation. Additionally, genetic association studies have tentatively connected *C6orf151* polymorphisms to metabolic disorders and neurodegenerative diseases, though causal mechanisms remain unexplored. Structural predictions propose potential membrane association or secretory pathways, but experimental validation is lacking.
Interest in C6orf151 has grown due to its possible relevance in cancer biology, with altered expression observed in certain tumors. However, comprehensive mechanistic insights and in vivo studies are still needed to define its molecular interactions and regulatory pathways. As an understudied protein, C6orf151 represents a frontier for discovering novel biomarkers or therapeutic targets, particularly in stress-related or metabolic diseases. Current research efforts focus on elucidating its interactome and functional roles using omics-based and cell-biological approaches.
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