| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C22orf15 |
| Uniprot No | Q8WYQ4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-132aa |
| 氨基酸序列 | MLCSQPGLANSSRVRGRVGTIRPVRCPSSSLHMSQRERTWPPPAMSPYWRTWMTITQSWQVSVRVQPRGRAHLLPNPYQQDFLGLPEELRRLSGLSSVGHNWRKRMGTRRGRHEQSPTSRPRKVSSLPPRSC |
| 分子量 | 41.6 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蛋白的假设性参考文献示例（若实际研究中文献不足，建议通过PubMed等数据库检索确认）：
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1. **文献名称**：*Structural and Functional Analysis of Human C22orf15 Protein Expressed in Escherichia coli*
**作者**：Zhang, L. et al.
**摘要**：本研究通过原核重组表达系统纯化人C22orf15蛋白，利用X射线晶体学解析其三维结构，揭示其可能参与核苷酸结合的折叠模式，并发现其在体外具有微弱的ATP酶活性。
2. **文献名称**：*C22orf15 Interaction with RNA Suggests a Role in Post-Transcriptional Regulation*
**作者**：Müller, R. et al.
**摘要**：通过重组C22orf15蛋白的体外结合实验，发现其特异性结合富含AU的RNA序列，提示其可能在mRNA稳定性或翻译调控中发挥作用，并通过CRISPR敲除模型验证其在细胞中的功能。
3. **文献名称**：*Dysregulation of C22orf15 in Neurodegenerative Disorders: Implications for Protein Aggregation*
**作者**：Chen, J. et al.
**摘要**：研究报道重组C22orf15蛋白在帕金森病患者脑脊液中表达异常，体外实验表明其错误折叠可能促进α-突触核蛋白聚集，暗示其与神经退行性病变的相关性。
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**注意事项**：
- 上述文献为假设性示例，C22orf15的研究可能仍属新兴领域，实际文献需通过学术数据库（如PubMed、Web of Science）以关键词“C22orf15”、“recombinant protein”等检索确认。
- 部分研究可能以预印本或未更名前的基因符号发表，建议扩展检索策略。
**Background of Recombinant Human (C22orf15) Protein**
The C22orf15 gene, located on human chromosome 22q13.1, encodes a poorly characterized protein initially identified through genomic sequencing. Though its precise biological function remains unclear, C22orf15 is suggested to play roles in cellular processes such as mitochondrial function, protein interaction networks, or nucleic acid metabolism based on domain predictions and limited experimental data. The protein contains conserved regions, including a putative coiled-coil domain, hinting at potential involvement in structural or regulatory complexes.
Recombinant C22orf15 protein is artificially produced using expression systems (e.g., *E. coli* or mammalian cells) for functional studies. Its recombinant form enables researchers to investigate its biochemical properties, subcellular localization, and interactions. Some studies link C22orf15 to human diseases; for instance, altered expression has been observed in cancers, though mechanistic insights are lacking. Additionally, murine homologs suggest possible roles in spermatogenesis or neural development, but these findings require validation in human systems.
Current research focuses on elucidating C22orf15's molecular interactions and pathways, leveraging techniques like mass spectrometry, CRISPR-based knockdown, or structural prediction tools. Despite its understudied status, interest in C22orf15 persists due to its evolutionary conservation and potential as a biomarker or therapeutic target. Further exploration is needed to unravel its physiological and pathological significance.
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