纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MYL2 |
Uniprot No | P10916 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-166aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MAPKKAKKRA GGANSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL NAFKVFDPEG KGVLKADYVR EMLTTQAERF SKEEVDQMFA AFPPDVTGNL DYKNLVHIIT HGEEKD |
预测分子量 | 21 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MYL2重组蛋白的模拟参考文献示例(仅供参考,具体文献需通过学术数据库核实):
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1. **文献名称**:*Recombinant MYL2 Expression in E. coli and Its Role in Cardiac Muscle Contraction*
**作者**:Smith J, et al.
**摘要**:本研究利用大肠杆菌表达系统成功制备了重组MYL2蛋白,并通过体外实验验证其与肌球蛋白重链的相互作用。研究发现,钙离子浓度变化显著影响MYL2的磷酸化状态,进而调节心肌收缩力,为肥厚型心肌病的机制研究提供了依据。
2. **文献名称**:*Structural Analysis of MYL2 Mutants Linked to Hypertrophic Cardiomyopathy*
**作者**:Chen L, Wang H.
**摘要**:通过X射线晶体学解析了MYL2重组蛋白及其两种致病突变体(R58Q和E143K)的三维结构。结果显示,突变导致蛋白构象改变,破坏其与肌球蛋白的结合能力,阐明了突变引发心肌功能障碍的结构基础。
3. **文献名称**:*Development of a MYL2 Recombinant Protein-Based Diagnostic Assay for Cardiomyopathy*
**作者**:Kumar S, et al.
**摘要**:基于重组MYL2蛋白开发了一种高灵敏度ELISA检测方法,用于筛查肥厚型心肌病患者血清中的特异性抗体。临床样本测试表明,该方法对早期诊断具有潜在应用价值。
4. **文献名称**:*Functional Characterization of MYL2 Phosphorylation Sites Using Recombinant Protein Technology*
**作者**:Garcia R, et al.
**摘要**:通过位点定向突变技术构建了MYL2重组蛋白的磷酸化位点突变体,并利用体外收缩模型证明Ser15和Ser20的磷酸化协同调控心肌细胞的收缩速率和力量,揭示了翻译后修饰在心脏功能中的关键作用。
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**注意**:以上文献信息为示例性内容,实际引用时请通过PubMed、Web of Science或Google Scholar等平台检索真实文献,并核对作者、标题及摘要准确性。
**Background of MYL2 Recombinant Protein**
MYL2 (myosin light chain 2) is a regulatory protein component of the myosin complex, essential for muscle contraction in cardiac and skeletal tissues. As part of the sarcomere, it binds to the heavy chain of myosin II, modulating ATPase activity and influencing the mechanical force generation during muscle contraction. MYL2 is particularly critical in cardiac muscle, where it plays a role in maintaining contractile efficiency and rhythm. Mutations in the MYL2 gene are associated with inherited cardiomyopathies, such as hypertrophic cardiomyopathy (HCM), highlighting its importance in cardiac health.
Recombinant MYL2 protein is produced using biotechnological methods, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian cells) to ensure proper post-translational modifications. The recombinant form retains the functional properties of native MYL2. enabling its use in structural studies, interaction assays, and mechanistic investigations of muscle contraction. It also serves as a tool for drug screening targeting MYL2-related pathologies or for developing diagnostic assays.
Research on MYL2 recombinant protein has advanced understanding of its role in disease mechanisms, particularly how specific mutations disrupt myosin dynamics, leading to impaired cardiac function. Additionally, it supports therapeutic development, including gene therapy and small-molecule interventions aimed at restoring normal myosin activity. Overall, MYL2 recombinant protein is a vital resource for both basic research and translational applications in cardiovascular biology.
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