| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LYRM1 |
| Uniprot No | O43325 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-122aa |
| 活性数据 | MTTATRQEVLGLYRSIFRLARKWQATSGQMEDTIKEKQYILNEARTLFRKNKNLTDTDLIKQCIDECTARIEIGLHYKIPYPRPIHLPPMGLTPLRGRGLRSQEKLRKLSKPVYLRSHDEVS |
| 分子量 | 13.5 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3条与重组人LYRM1蛋白相关的参考文献概览：
1. **《LYRM1 regulates mitochondrial metabolism and protects against oxidative stress in mammalian cells》**
*作者：Smith A, et al. (2020)*
摘要：本研究通过原核系统表达重组人LYRM1蛋白，发现其作为线粒体复合物III的组装辅助因子，调控能量代谢并减少活性氧积累，提示其在神经退行性疾病中的潜在作用。
2. **《Crystal structure of human LYRM1 reveals a conserved leucine-rich motif for protein interactions》**
*作者：Li J, et al. (2018)*
摘要：解析了重组LYRM1蛋白的晶体结构，揭示其富含亮氨酸的结构域与多种线粒体蛋白互作的分子机制，为研究代谢疾病相关突变提供结构依据。
3. **《Recombinant LYRM1 enhances adipocyte differentiation via AMPK signaling pathway》**
*作者：Wang H, et al. (2019)*
摘要：利用哺乳动物细胞表达重组LYRM1.证明其通过激活AMPK通路促进脂肪细胞分化，并调节葡萄糖摄取，可能与肥胖及2型糖尿病发病相关。
备注：以上为领域内常见研究方向(结构、代谢、疾病关联)的示例，实际文献需通过PubMed/Google Scholar检索验证。LYRM1相关研究相对较少，建议扩展搜索其别名(如C6ORF222)或功能关键词(如“线粒体复合物III”“能量代谢”)。
The human LYRM1 protein, also known as LYR motif-containing protein 1. is a mitochondrial protein implicated in iron-sulfur (Fe-S) cluster biosynthesis and cellular metabolic regulation. It belongs to the LYRM family characterized by a conserved leucine-tyrosine-arginine motif (LYR motif), which facilitates protein-protein interactions and binding to Fe-S cofactors. LYRM1 is reported to interact with mitochondrial complex II (succinate dehydrogenase), serving as an assembly chaperone or stability factor. Its role in Fe-S cluster transfer is critical for electron transport chain functionality and redox homeostasis. Recombinant human LYRM1 protein is typically produced in E. coli or mammalian expression systems for functional studies. Research focuses on elucidating its structural dynamics, interactions with partner proteins like SDHAF1. and implications in metabolic disorders, neurodegenerative diseases, and cancer. Dysregulation of LYRM1 has been associated with mitochondrial dysfunction and oxidative stress, making it a potential biomarker or therapeutic target. Current studies employ techniques like co-immunoprecipitation, X-ray crystallography, and gene knockout models to explore its mechanistic contributions to cellular respiration and Fe-S cluster biogenesis.
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