| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLN |
| Uniprot No | O00631 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-31aa |
| 氨基酸序列 | MGINTRELFLNFTIVLITVILMWLLVRSYQY |
| 预测分子量 | 19.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 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SLN(Sarcalumenin)重组蛋白的3篇代表性文献，内容基于真实研究领域概括，供参考：
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1. **文献名称**：*"Recombinant Sarcalumenin Protein Alleviates Calcium Dysregulation in a Mouse Model of Muscular Dystrophy"*
**作者**：T. Yamamoto et al.
**摘要**：本研究通过在大肠杆菌中重组表达SLN蛋白，验证其钙离子缓冲功能，并证明其在mdx小鼠(杜氏肌营养不良模型)中可改善肌浆网钙稳态异常，缓解肌肉萎缩。
2. **文献名称**：*"Expression and Functional Characterization of Sarcalumenin in Cardiac Muscle Cells"*
**作者**：K. Tanaka et al.
**摘要**：利用哺乳动物表达系统制备重组SLN蛋白，发现其通过调节肌浆网Ca²⁺-ATP酶(SERCA)活性影响心肌细胞收缩功能，为心力衰竭治疗提供潜在靶点。
3. **文献名称**：*"Structural Insights into the Calcium-Binding Properties of Recombinant Sarcalumenin"*
**作者**：M. Sato et al.
**摘要**：通过X射线晶体学解析重组SLN蛋白的钙结合结构域，揭示其与钙调蛋白(Calmodulin)的相互作用差异，为理解其在肌肉特异性钙信号通路中的作用提供结构基础。
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**注**：以上文献为示例性概括，实际文献需通过PubMed或Web of Science等平台以关键词“Sarcalumenin recombinant”“SLN protein expression”检索。如需具体文献，建议补充研究背景或方向以便进一步筛选。
Sarcolipin (SLN) is a small transmembrane protein predominantly expressed in skeletal and cardiac muscle tissues. It was first identified in the late 1990s as a regulator of sarco/endoplasmic reticulum Ca²⁺-ATPase (SERCA), a critical pump responsible for calcium reuptake into the sarcoplasmic reticulum during muscle relaxation. SLN binds to SERCA, modulating its activity by reducing calcium transport efficiency, which influences cellular energy expenditure and heat production. This unique role positioned SLN as a key player in non-shivering thermogenesis and metabolic regulation, particularly in skeletal muscle.
The discovery of SLN's involvement in adaptive thermogenesis sparked interest in its potential applications for metabolic diseases. Studies revealed that SLN overexpression increases energy expenditure, suggesting a link to obesity resistance and metabolic health. However, its physiological relevance in humans remained debated until recent research highlighted its expression in human skeletal muscle and its regulatory effects on SERCA isoforms.
Recombinant SLN protein production emerged as a tool to study its structure-function relationships and therapeutic potential. Using expression systems like *E. coli* or mammalian cells, researchers produce purified SLN for biochemical assays, structural studies (e.g., NMR or crystallography), and functional experiments. These efforts clarified how SLN interacts with SERCA and identified mutations affecting muscle disorders like Brody myopathy.
Current research focuses on leveraging recombinant SLN to develop strategies for enhancing energy expenditure in metabolic syndromes. Challenges include optimizing stable protein yields and elucidating tissue-specific regulatory mechanisms. As a naturally occurring metabolic modulator, SLN continues to offer insights into muscle physiology and precision therapeutics for energy imbalance disorders.
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