| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPEG |
| Uniprot No | Q15772 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-113aa |
| 氨基酸序列 | MQKARGTRGEDAGTRAPPSPGVPPKRAKVGAGGGAPVAVAGAPVFLRPLKNAAVCAGSDVRLRVVVSGTPQPSLRWFRDGQLLPAPAPEPSCLWLRRCGAQDAGVYSCMAQNE |
| 预测分子量 | 38.7kDa |
| 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SPEG重组蛋白的3篇代表性文献概览：
1. **《SPEG Interactions with Regulatory Proteins in Cardiac Muscle》**
- 作者：Liu X, et al.
- 摘要：研究通过重组SPEG蛋白表达，揭示了其在心肌细胞中与肌浆网钙调控蛋白(如SERCA2a)的相互作用机制，证明SPEG磷酸化修饰对心脏收缩功能的关键作用。
2. **《Recombinant SPEG Kinase Improves Skeletal Muscle Regeneration in Murine Models》**
- 作者：Smith J, et al.
- 摘要：利用大肠杆菌系统成功表达功能性重组SPEG激酶，并在肌肉损伤模型中验证其通过激活mTOR通路促进肌管分化和修复的潜力。
3. **《Structural Insights into SPEG Complex Formation via Cryo-EM》**
- 作者：Chen L, et al.
- 摘要：通过冷冻电镜解析重组SPEG蛋白与结合伴侣的结构，阐明其激酶结构域的自抑制机制及病理突变(如心肌病相关突变)对蛋白活性的影响。
注：以上内容为模拟文献概览，实际文献需通过PubMed/Google Scholar检索确认。若需具体文章，可补充关键词(如疾病模型、物种等)进一步筛选。
**Background of SPEG Recombinant Protein**
SPEG (Striated muscle preferentially expressed protein kinase) is a serine/threonine kinase predominantly expressed in cardiac and skeletal muscle tissues. Discovered in the early 2000s, SPEG belongs to the calcium/calmodulin-dependent protein kinase family and plays a critical role in muscle development, function, and maintenance. Structurally, SPEG contains tandem kinase domains, distinguishing it from other kinases, and is essential for proper sarcomere formation, calcium handling, and cardiomyocyte maturation. Its dysfunction has been linked to severe human pathologies, including congenital myopathies and cardiomyopathies, underscoring its biological significance.
Recombinant SPEG protein is engineered using heterologous expression systems (e.g., *E. coli*, mammalian cells*) to produce purified, functional kinase for research and therapeutic applications. The recombinant form retains enzymatic activity, enabling studies on its phosphorylation targets, interaction partners, and regulatory mechanisms. Advances in protein engineering, such as affinity tags (e.g., His-tag, GST-tag), enhance purification efficiency and yield, ensuring high-quality protein for structural and functional analyses.
Research on SPEG recombinant protein has expanded insights into muscle biology and disease mechanisms. For instance, studies using recombinant SPEG have elucidated its role in modulating proteins like junctophilin-2. critical for maintaining cardiac muscle integrity. Additionally, SPEG’s involvement in neonatal heart development has made it a potential therapeutic target for pediatric cardiomyopathies.
The development of SPEG recombinant proteins also supports drug discovery, enabling high-throughput screening for kinase inhibitors or activators. Furthermore, its use in disease modeling (e.g., CRISPR-edited cell lines) helps bridge gaps between genetic mutations and clinical phenotypes.
Overall, SPEG recombinant protein serves as a vital tool in cardiovascular and musculoskeletal research, offering avenues to explore novel treatments for muscle-related disorders while advancing our understanding of kinase biology in health and disease.
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