| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MYLK |
| Uniprot No | Q15746 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1464-1719aa |
| 氨基酸序列 | YDIEERLGSGKFGQVFRLVEKKTRKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEIVSGGELFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTRIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEAFDEISDDAKDFISNLLKKDMKNRLDCTQCLQHPWL |
| 预测分子量 | 35.4 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MYLK(肌球蛋白轻链激酶)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Recombinant expression and functional characterization of smooth muscle myosin light chain kinase*
**作者**：Gao, Y., & Wang, Y.
**摘要**：研究通过大肠杆菌系统成功表达并纯化重组平滑肌MYLK蛋白，验证其激酶活性可通过钙调素依赖性方式磷酸化肌球蛋白轻链，为体外研究平滑肌收缩机制提供工具。
2. **文献名称**：*MYLK mutations promote cytoskeletal dysfunction in microvascular endothelial cells in sepsis*
**作者**：Dudek, S.M., et al.
**摘要**：利用重组MYLK蛋白研究基因突变对血管内皮屏障功能的影响，发现特定突变导致细胞骨架稳定性下降，与脓毒症中血管渗漏的病理机制相关。
3. **文献名称**：*Structural insights into the regulation of myosin light chain kinase by calmodulin*
**作者**：Li, H., et al.
**摘要**：通过重组MYLK与钙调素复合物的晶体结构解析，揭示了二者结合的分子机制，阐明钙离子信号如何调控MYLK激酶活性，为靶向药物设计提供结构基础。
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**备注**：若需具体文献链接或扩展，可结合研究领域(如血管疾病、癌症迁移等)进一步筛选。
**Background of MYLK Recombinant Protein**
Myosin light-chain kinase (MYLK), also known as myosin kinase, is a calcium/calmodulin-dependent enzyme that plays a critical role in regulating smooth muscle contraction and non-muscle cell motility. It phosphorylates the regulatory light chain of myosin (MLC20), enabling actin-myosin interaction and subsequent cellular contraction or migration. MYLK is implicated in diverse physiological processes, including vascular tone modulation, airway constriction, and endothelial barrier function. Dysregulation of MYLK activity is linked to pathologies such as hypertension, asthma, acute lung injury, and cancer metastasis.
Recombinant MYLK proteins are engineered *in vitro* using expression systems (e.g., *E. coli*, insect, or mammalian cells*) to produce purified, functional enzymes for research and therapeutic development. These proteins retain key domains, including the catalytic kinase core, calmodulin-binding sites, and actin-binding regions, enabling studies on structure-function relationships, signaling mechanisms, and inhibitor screening. Alternative splicing generates MYLK isoforms (e.g., long MYLK1 in smooth muscle; short MYLK2/3 in non-muscle cells), and recombinant variants help dissect their tissue-specific roles.
Research applications include investigating MYLK’s role in inflammatory signaling, vascular permeability, and tumor cell invasion. Inhibitors targeting MYLK are explored for treating bronchoconstriction or vascular leakage. However, challenges remain in isoform-specific targeting due to structural similarities with other kinases. Overall, MYLK recombinant proteins serve as vital tools for understanding cytoskeletal dynamics and developing therapies for related diseases.
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