| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C9orf45 |
| Uniprot No | 0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-167aa |
| 氨基酸序列 | MVRPALHKQVLFTAHPHFLDGVLSTAFPLAHFMWQLLRDGTYHGCGRCFATTYYLSEGGGLIFRNVTGEPNCRPPTRGPRSLHLPGTKGSSGSLRSCLQPPGGRPFQHTRAYGGKMKAGPRGNSLLLSFPWADTIYFLAPSSVYPVFPKASLDSGLSSWTHLSGLLC |
| 分子量 | 44.6 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C9orf45蛋白的模拟参考文献示例(注：因该蛋白研究较少，以下内容为假设性示例，建议通过专业数据库获取真实文献)：
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1. **文献名称**: *Cloning and functional analysis of human C9orf45 protein in cell cycle regulation*
**作者**: Zhang L. et al. (2018)
**摘要**: 研究报道了C9orf45基因的克隆及其重组蛋白的表达纯化，发现其在HeLa细胞中调控G1/S期转换，可能通过相互作用周期蛋白依赖性激酶(CDKs)发挥作用。
2. **文献名称**: *Structural insights into the enzymatic activity of C9orf45 through X-ray crystallography*
**作者**: Smith J. et al. (2020)
**摘要**: 首次解析了重组人C9orf45蛋白的晶体结构，揭示其N端结构域具有非典型ATP酶活性，为探究其生物学功能提供了结构基础。
3. **文献名称**: *C9orf45 deficiency promotes tumorigenesis via modulating mTOR signaling*
**作者**: Wang Y. et al. (2021)
**摘要**: 通过敲低C9orf45的细胞模型和小鼠实验，证明该蛋白通过抑制mTOR通路发挥抑癌作用，重组蛋白的过表达可延缓肿瘤生长。
4. **文献名称**: *C9orf45 interacts with mitochondrial proteins and impacts oxidative stress response*
**作者**: Kim S. et al. (2019)
**摘要**: 利用重组C9orf45蛋白进行免疫共沉淀实验，发现其定位于线粒体并与超氧化物歧化酶(SOD2)结合，可能参与氧化应激调控。
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**注意**：以上内容为模拟生成，C9orf45的实际研究可能有限，建议通过PubMed或Google Scholar等平台以“C9orf45 protein”“recombinant C9orf45”等关键词检索最新文献。
The recombinant human C9orf45 protein is derived from the C9orf45 gene (Chromosome 9 Open Reading Frame 45), a poorly characterized protein-coding gene located on chromosome 9p13.3. Despite its identification through genomic sequencing, the precise biological function of C9orf45 remains unclear, though it is speculated to play roles in cellular processes such as proliferation, differentiation, or stress responses. The protein is predicted to contain multiple α-helices and disordered regions, suggesting potential interactions with other biomolecules, though experimental validation is limited. Recombinant C9orf45 is typically produced in heterologous systems (e.g., E. coli, mammalian cells) to enable functional studies, given its low endogenous expression in tissues. Current research focuses on elucidating its involvement in disease contexts, with preliminary links to cancer progression and neurological disorders, possibly through modulation of signaling pathways like MAPK or Wnt. However, mechanistic details remain elusive, partly due to the lack of specific antibodies or validated interaction partners. Structural studies using recombinant protein aim to resolve its 3D conformation and identify functional domains. Emerging evidence also suggests potential roles in transcriptional regulation or RNA metabolism, based on in silico analyses of conserved motifs. Further characterization of recombinant C9orf45 could clarify its physiological relevance and therapeutic potential.
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