| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C22orf25 |
| Uniprot No | Q6ICL3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-276aa |
| 氨基酸序列 | MCIIFFKFDPRPVSKNAYRLILAANRDEFYSRPSKLADFWGNNNEILSGLDMEEGKEGGTWLGISTRGKLAALTNYLQPQLDWQARGRGELVTHFLTTDVDSLSYLKKVSMEGHLYNGFNLIAANLSTAKGDVICYYGNRGEPDPIVLTPGTYGLSNALLETPWRKLCFGKQLFLEAVERSQALPKDVLIASLLDVLNNKEAQLPDPAIEDQGGEYVQPMLSKYAAVCVRCPGYGTRTNTIILVDADGHVTFTERSMMDKDLSHWETRTYEFTLQS |
| 分子量 | 57.3 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C22orf25蛋白的3篇示例参考文献（虚构内容，仅供参考）：
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1. **文献名称**: *Structural characterization of recombinant human C22orf25 reveals a conserved protein interaction domain*
**作者**: Smith J, et al.
**摘要**: 本研究利用X射线晶体学解析了重组人C22orf25蛋白的三维结构，揭示了其N端保守的α-螺旋结构域可能在蛋白质相互作用中发挥关键作用，为后续功能研究提供结构基础。
2. **文献名称**: *C22orf25 regulates cell cycle progression via interaction with CDK2 in human cells*
**作者**: Lee H, et al.
**摘要**: 通过免疫共沉淀和RNA干扰实验，发现重组表达的C22orf25蛋白与细胞周期蛋白CDK2直接结合，敲低C22orf25导致G1/S期阻滞，提示其在细胞周期调控中的潜在功能。
3. **文献名称**: *Recombinant C22orf25 expression in E. coli: optimization and enzymatic activity screening*
**作者**: Patel R, et al.
**摘要**: 开发了一种高效原核表达系统，实现重组人C22orf25蛋白的可溶性纯化，并通过体外酶活性筛选发现其可能具有弱ATP水解酶活性，需进一步验证功能。
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**备注**：以上内容为示例，实际文献需通过数据库（如PubMed、Google Scholar）检索。若研究较少，可扩展至C22orf25基因的调控机制或疾病关联文献。建议结合EndNote或Zotero等工具管理参考文献格式。
C22orf25, a human protein encoded by the open reading frame 25 on chromosome 22, remains poorly characterized, though emerging studies highlight its potential roles in cellular processes. Structurally, it is predicted to contain conserved domains linked to nucleic acid binding or enzymatic activity, suggesting involvement in DNA/RNA metabolism. Transcriptomic data indicate widespread but variable expression across tissues, with higher levels observed in the brain, testes, and immune cells, hinting at tissue-specific functions. Subcellular localization studies propose its presence in the nucleus and cytoplasm, aligning with putative roles in gene regulation or signaling pathways.
Recombinant C22orf25 protein, produced via heterologous expression systems (e.g., E. coli or mammalian cells), enables functional and structural analyses. Recent proteomic studies identify interactions with proteins involved in mRNA splicing, chromatin remodeling, and stress responses, positioning it as a potential modulator of these pathways. Notably, dysregulation of C22orf25 has been tentatively associated with neurological disorders and certain cancers, though mechanistic insights remain limited.
Despite its enigmatic nature, C22orf25 is increasingly recognized for its evolutionary conservation across vertebrates, underscoring biological significance. Ongoing research focuses on delineating its molecular interactions, enzymatic properties (if any), and disease relevance. Advances in CRISPR-based screening and multi-omics approaches are expected to clarify its contributions to cellular homeostasis and pathology.
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