| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C22orf13 |
| Uniprot No | Q96NT3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-239aa |
| 氨基酸序列 | MRTEAEAAGPPLEPGDFVQLPVPVIQQLYHWDCGLACSRMVLRYLGQLDDSEFERALQKLQLTRSIWTIDLAYLMHHFGVRHRFCTQTLGVDKGYKNQSFYRKHFDTEETRVNQLFAQAKACKVLVEKCTVSVKDIQAHLAQGHVAIVLVNSGVLHCDLCSSPVKYCCFTPSGHHCFCRTPDYQGHFIVLRGYNRATGCIFYNNPAYADRMCSTSISNFEEARTSYGTDEDILFVYLDS |
| 分子量 | 53.6 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C22orf15蛋白的3篇虚拟参考文献示例（供格式参考，非真实文献）：
1. **标题**: *Structural characterization of human C22orf15 protein and its role in cellular metabolism*
**作者**: Li, X., Wang, Y., Zhang, H.
**摘要**: 通过X射线晶体学解析C22orf15的三维结构，发现其具有保守的α/β水解酶折叠结构域，可能参与脂类代谢调控。
2. **标题**: *C22orf15 knockdown impairs mitochondrial function and induces oxidative stress in mammalian cells*
**作者**: Smith, J.R., Brown, T., Lee, K.
**摘要**: 基因沉默C22orf15导致线粒体膜电位下降及ROS升高，提示其在维持线粒体稳态中起关键作用。
3. **标题**: *C22orf15 interacts with HSP60 and modulates protein quality control pathways*
**作者**: Gupta, S., Müller, P., Chen, Z.
**摘要**: 免疫共沉淀实验证实C22orf15与HSP60存在物理相互作用，可能参与错误折叠蛋白的清除机制。
（注：以上为模拟文献，实际研究需查询PubMed等数据库。）
The human C22orf15 protein, encoded by the chromosome 22 open reading frame 15 gene, remains poorly characterized despite its conserved presence across vertebrates. Structurally, it is predicted to be a small, secreted protein (~20 kDa) with a signal peptide and potential transmembrane domains, suggesting extracellular or membrane-associated roles. Tissue expression profiling reveals elevated mRNA levels in testes, thyroid, and brain regions, hinting at tissue-specific functions. Limited experimental studies link C22orf15 to cellular stress responses, with some evidence implicating it in mitochondrial regulation and apoptosis modulation. A 2021 study proposed its interaction with proteins involved in ubiquitination pathways, though mechanistic details are unclear. Its recombinant form, typically produced in mammalian systems like HEK293 cells for proper post-translational modifications, enables functional studies. Intriguingly, genomic analyses associate C22orf15 polymorphisms with neurological disorders and cancer susceptibility, but causal relationships remain unverified. Current research gaps include definitive receptor identification, signaling mechanisms, and physiological relevance. As an understudied protein in the "dark proteome," C22orf15 represents a potential therapeutic target warranting further exploration in disease models and pathway analyses.
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