| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | C22orf33 |
| Uniprot No | O43247 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-195aa |
| 氨基酸序列 | MDPQSRSLKNAGSRSSSRENRATSGEGAQPCQGTDDGPSLGAQDQRSTPTNQKGSIIPNNIRHKFGSNVVDQLVSEEQAQKAIDEVFEGQKRASSWPSRTQNPVEISSVFSDYYDLGYNMRSNLFRGAAEETKSLMKASYTPEVIEKSVRDLEHWHGRKTDDLGRWHQKNAMNLNLQKALEEKYGENSKSKSSKY |
| 分子量 | 48.2 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. |
1. **《C22orf33的结构表征及其与线粒体代谢的关联》**
- 作者：Smith A, et al.
- 摘要：通过冷冻电镜解析了重组人C22orf33蛋白的三维结构，发现其通过结合线粒体膜蛋白调控ATP代谢，提示其在能量代谢疾病中的潜在作用。
2. **《C22orf33在癌症细胞增殖中的功能研究》**
- 作者：Wang X, et al.
- 摘要：通过CRISPR敲除实验证明，C22orf33通过抑制mTOR信号通路抑制癌细胞增殖，表明其可能作为肿瘤治疗的靶点。
3. **《重组C22orf33蛋白的互作组学分析揭示其神经发育功能》**
- 作者：Li J, et al.
- 摘要：利用质谱技术鉴定C22orf33与突触后蛋白复合物相互作用，提示其参与神经突触形成和发育障碍相关疾病。
4. **《C22orf33基因敲除小鼠模型揭示其胚胎致死性》**
- 作者：Garcia R, et al.
- 摘要：构建C22orf33缺陷小鼠模型，发现胚胎早期致死表型，结合转录组学分析表明该蛋白对胚胎干细胞分化至关重要。
*注：以上文献信息为示例性虚构，实际研究中请查阅PubMed/NCBI等数据库获取真实数据。*
**Background of Recombinant Human C22orf33 Protein**
The C22orf33 protein, encoded by the open reading frame C22orf33 located on human chromosome 22, remains poorly characterized, though recent studies suggest its involvement in fundamental cellular processes. The gene is evolutionarily conserved, implying potential functional significance. Bioinformatic analyses predict that the protein contains disordered regions and possible phosphorylation sites, hinting at roles in signaling or regulatory pathways. Experimental data are limited, but proteomic studies have linked C22orf33 to RNA-binding proteins and components of stress granules, suggesting a possible role in RNA metabolism or stress response.
Recombinant human C22orf33 protein is typically produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for biochemical and functional studies. Its recombinant form enables investigations into structure-function relationships, interactome mapping, and validation of putative enzymatic or regulatory activities. Some studies associate C22orf33 dysregulation with diseases, including cancer, though mechanistic insights are lacking. Current research focuses on elucidating its molecular interactions, post-translational modifications, and relevance to cellular homeostasis or pathology. Despite its enigmatic nature, C22orf33 represents a target for exploratory studies aimed at uncovering novel biological pathways or therapeutic opportunities.
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