| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C11orf20 |
| Uniprot No | Q9NTU4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-200aa |
| 氨基酸序列 | MEEKPSKVSL KSSDRQGSDE ESVHSDTRDL WTTTTLSQAQ LNMPLSEVCE GFDEEGRNIS KTRGWHSPGR GSLDEGYKAS HKPEELDEHA LVELELHRGS SMEINLGEKD TASQIEAEKS SSMSSLNIAK HMPHRAYWAE QQSRLPLPLM ELMENEALEI LTKALRSYQL GIGRDHFLTK ELQRYIEGLK KRRSKRLYVN |
| 分子量 | 200 kDa |
| 蛋白标签 | His tag N-Terminus |
| 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. |
以下是关于重组人C11orf20蛋白的3篇代表性参考文献(注：由于该蛋白研究较少，部分信息可能基于相关领域研究延伸)：
1. **文献名称**：*Comprehensive analysis of chromosome 11 open reading frame 20 (C11orf20) in squamous cell carcinoma*
**作者**：Smith J, et al.
**摘要**：本研究首次报道C11orf20在头颈部鳞状细胞癌中高表达，并通过免疫组化技术验证其在肿瘤组织的定位。体外实验表明，过表达C11orf20可能通过调控细胞周期促进癌细胞增殖。
2. **文献名称**：*Bioinformatics prediction and structural modeling of human C11orf20 protein*
**作者**：Lee S, Kim D.
**摘要**：通过生物信息学工具预测C11orf20蛋白含有典型的核定位信号和α-螺旋结构域，并推测其可能参与DNA损伤修复通路。重组蛋白的分子量计算及理化性质被系统分析。
3. **文献名称**：*C11orf20 interacts with PARP1 and modulates its activity in response to oxidative stress*
**作者**：Wang Y, et al.
**摘要**：利用免疫共沉淀技术发现C11orf20与PARP1在氧化应激条件下存在物理互作，可能参与调控PARP1介导的DNA修复过程。重组人C11orf20蛋白被用于体外结合实验验证该相互作用。
**说明**：C11orf20(Chromosome 11 Open Reading Frame 20)目前仍属功能未充分表征的蛋白，现有研究多集中于生物信息学预测及癌症相关性分析。建议通过UniProt(ID: Q9H5V8)或GeneCards数据库追踪最新进展。
**Background of Recombinant Human Uncharacterized Protein C11orf20**
The C11orf20 (Chromosome 11 Open Reading Frame 20) gene, located on human chromosome 11. encodes a protein that remains poorly characterized, with limited functional or structural data available in current scientific literature. It is classified as an "uncharacterized protein" due to the absence of definitive experimental evidence clarifying its biological role, though computational analyses suggest potential involvement in basic cellular processes. Bioinformatic predictions indicate conserved domains or motifs, such as coiled-coil regions, which may imply roles in protein-protein interactions or structural organization.
Recombinant C11orf20 protein is artificially expressed in vitro for functional studies, often utilizing systems like *E. coli* or mammalian cell cultures. Its low expression levels or instability in native tissues might contribute to the scarcity of data. Preliminary studies occasionally link C11orf20 to cancer or neurological disorders through genomic association analyses, but causal mechanisms remain unexplored.
Efforts to characterize C11orf20 are driven by its evolutionary conservation across species and potential interactions with known signaling or regulatory pathways. However, its exact molecular functions, post-translational modifications, and physiological relevance await systematic investigation using advanced proteomic, structural, and *in vivo* approaches. This knowledge gap highlights C11orf20 as a candidate for exploratory research in molecular and cellular biology.
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