| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LOC730092 |
| Uniprot No | 0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-152aa |
| 活性数据 | MGFAEAFLEHLWKNLQDPSNPAIIRQAAGNYIGSFLARAKFISLITVKPCLDLLVNWLHIYLNNQDSGTKAFCDVALHGPFYSACQAVFYTFVFRHKQLLSGNLKEGLQYPQSLNFERIVMSQLNPLKICLPSVVNFFAAITKMKTCGYGWW |
| 分子量 | 43.7 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. |
由于目前关于“LOC730092”这一基因/蛋白的公开研究数据非常有限，且其功能尚未被广泛研究，目前公开数据库中暂未检索到明确以“重组人LOC730092蛋白”为主题的文献。以下是模拟生成的结构参考范例(假设性内容，仅供理解格式)：
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1. **标题**: *Expression and purification of recombinant human LOC730092 protein in E. coli system*
**作者**: Zhang L. et al.
**摘要**: 本研究首次在大肠杆菌系统中实现了人源LOC730092蛋白的重组表达，通过优化密码子和纯化条件获得高纯度蛋白，并验证其体外稳定性。
2. **标题**: *Structural characterization of LOC730092 reveals a potential role in mitochondrial metabolism*
**作者**: Smith J. et al.
**摘要**: 通过X射线晶体学解析LOC730092的三维结构，发现其具有与代谢酶相似的活性位点，推测参与线粒体能量代谢调控。
3. **标题**: *LOC730092 interacts with p53: implications in cancer cell apoptosis*
**作者**: Wang Y. et al.
**摘要**: 利用免疫共沉淀技术证明LOC730092与p53蛋白直接结合，可能通过影响p53信号通路参与癌细胞凋亡过程。
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**注意事项**：
- **LOC730092** 属于NCBI数据库中暂未明确功能注释的基因编号，建议访问 **UniProt(https://www.uniprot.org)** 或 **PubMed(https://pubmed.ncbi.nlm.nih.gov)** 检索最新进展。
- 若需研究此蛋白，可结合同源蛋白分析或实验验证其功能。
Recombinant human LOC730092 protein is a genetically engineered form of a hypothetical protein encoded by the LOC730092 gene, currently annotated in human genomic databases. This locus is classified as a non-coding RNA gene in some references but may have a putative protein-coding transcript, reflecting ongoing updates in genomic annotation. The protein’s precise biological function remains uncharacterized due to limited experimental evidence. However, in silico analyses suggest potential structural motifs, such as transmembrane domains or conserved regions, which hint at roles in cellular signaling or molecular interactions.
The recombinant version is typically produced in heterologous expression systems (e.g., E. coli or mammalian cells) to enable functional studies. Its production facilitates investigations into its subcellular localization, protein-protein interactions, and possible involvement in physiological or pathological processes. Research interest in LOC730092 may stem from its differential expression patterns observed in transcriptomic datasets related to specific diseases or developmental stages, though these associations remain speculative.
As with many understudied proteins, challenges include validating its expression in vivo and distinguishing its functions from homologous proteins. Current applications of recombinant LOC730092 focus on generating antibodies, structural characterization, and initial biochemical assays to elucidate its role in human biology. Further research is essential to clarify its significance in cellular mechanisms or potential as a therapeutic target.
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