| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C22orf23 |
| Uniprot No | Q9BZE7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-217aa |
| 氨基酸序列 | MASQKQMEVVTKGTGFRRRPKTITYTPGTCELLRVMMKESKLTNIQQRHIMDIMKRGDALPLQCSPTSSQRVLPSKQIASPIYLPPILAARPHLRPANMCQANGAYSREQFKPQATRDLEKEKQRLQNIFATGKDMEERKRKAPPARQKAPAPELDRFEELVKEIQERKEFLADMEALGQGKQYRGIILAEISQKLREMEDIDHRRSEELRKGLATT |
| 分子量 | 50.27 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C22orf23蛋白的3篇文献摘要简述：
1. **文献名称**：*Characterization of C22orf23 as a novel nuclear pore complex-interacting protein*
**作者**：Smith A, et al.
**摘要**：研究鉴定了C22orf23作为核孔复合体（NPC）的新型互作蛋白，利用重组表达技术证明其通过与NPC组分结合参与核质运输调控，并揭示其序列中保守的结构域功能。
2. **文献名称**：*Functional analysis of C22orf23 in DNA damage response*
**作者**：Lee J, et al.
**摘要**：通过重组C22orf23蛋白的体外实验，发现其与DNA修复因子相互作用，在电离辐射后定位至损伤位点，提示其在基因组稳定性维持中的潜在作用。
3. **文献名称**：*Expression and purification of recombinant human C22orf23 for structural studies*
**作者**：Zhang Y, et al.
**摘要**：报道了在大肠杆菌中高效表达并纯化重组C22orf23蛋白的优化方法，为后续结晶及结构解析提供基础，同时验证了其寡聚化倾向。
注：以上为模拟示例，实际文献需通过数据库（如PubMed）检索确认。该基因可能属于NPIP家族，建议同时尝试其别名（如NPIPB9）扩展搜索。
The human C22orf23 protein, encoded by the chromosome 22 open reading frame 23 gene, is a poorly characterized protein with limited functional annotation in current scientific literature. It is conserved across vertebrates, suggesting potential biological relevance, though its specific molecular mechanisms remain unclear. The protein is predicted to contain a transmembrane domain and localize to intracellular membranes, possibly the endoplasmic reticulum or Golgi apparatus. Structural analyses indicate a conserved DUF4761 domain, which is linked to proteins of unknown function.
Experimental studies are sparse, but high-throughput data hint at roles in cellular processes like protein trafficking, cell cycle regulation, or lipid metabolism. C22orf23 shows tissue-specific expression patterns, with higher levels in the brain, testis, and secretory organs. Dysregulation has been weakly associated with cancers, neurodegenerative diseases, and ciliopathies in preliminary studies, though no direct pathological mechanisms are established. Its interaction partners include vesicle transport proteins and enzymes, supporting hypothetical involvement in membrane dynamics. Current research gaps highlight the need for functional assays (e.g., CRISPR knockouts, interactome mapping) to clarify its physiological and disease-related significance. Despite limited knowledge, C22orf23 is occasionally flagged in omics studies as a potential biomarker or therapeutic target candidate.
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