纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | MYL1 |
Uniprot No | P05976 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 3-142aa |
氨基酸序列 | PKKDVKKP VAAAAAAPAP APAPAPAPAP AKPKEEKIDL SAIKIEFSKE QQDEFKEAFL LFDRTGDSKI TLSQVGDVLR ALGTNPTNAE VRKVLGNPSN EELNAKKIEF EQFLPMMQAI SNNKDQATYE DFVEGLRVFD KE |
预测分子量 | 17 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MYL1重组蛋白的3篇参考文献的简要整理:
1. **文献名称**:*"Recombinant expression and functional characterization of human myosin light chain-1 in Escherichia coli"*
**作者**:K. Yamashita et al.
**摘要**:本研究成功在大肠杆菌中表达并纯化了重组人MYL1蛋白,通过体外ATP酶活性实验证实其可有效结合肌球蛋白重链,并增强肌球蛋白复合体的收缩功能,为后续结构研究奠定基础。
2. **文献名称**:*"Phosphorylation-dependent regulation of skeletal muscle myosin light chain-1 via recombinant protein analysis"*
**作者**:J.T. Stull et al.
**摘要**:通过重组MYL1蛋白实验,揭示了钙/钙调素依赖性激酶(CaMK)对其特定丝氨酸残基的磷酸化修饰,可显著调控肌球蛋白ATP酶活性及肌肉收缩动力学。
3. **文献名称**:*"Structural insights into MYL1 mutations linked to congenital myopathy using recombinant protein crystallography"*
**作者**:A. Houdusse et al.
**摘要**:利用重组MYL1蛋白的晶体结构解析,发现某些先天性肌病相关突变会破坏其与肌球蛋白重链的相互作用,导致肌纤维组装异常,为病理机制提供分子层面解释。
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**注**:以上文献信息为示例性虚构,实际文献需通过PubMed/Google Scholar等平台检索关键词(如"MYL1 recombinant protein"、"myosin light chain 1 expression")获取。
**Background of MYL1 Recombinant Protein**
MYL1 (Myosin Light Chain 1) is a critical regulatory component of myosin, a motor protein essential for muscle contraction and cellular motility. It belongs to the myosin light chain family, which modulates the ATPase activity of myosin heavy chains, influencing the mechanical properties of actin-myosin interactions. MYL1 is specifically expressed in skeletal muscle and plays a pivotal role in fast-twitch muscle fibers, contributing to rapid, forceful contractions. Its function is tightly regulated through phosphorylation, which alters myosin’s conformation and activity during muscle activation.
Recombinant MYL1 protein is produced using biotechnological methods, such as *E. coli* or mammalian expression systems, to ensure high purity and biological activity. This involves cloning the MYL1 gene into expression vectors, followed by protein synthesis, purification (e.g., affinity chromatography), and validation via techniques like SDS-PAGE and Western blotting. Recombinant MYL1 retains the ability to bind myosin heavy chains and regulate contraction, making it invaluable for *in vitro* studies.
Research applications include investigating muscle physiology, neuromuscular disorders (e.g., myopathies), and drug screening for conditions linked to aberrant muscle function. Additionally, MYL1 serves as a model to study mutations affecting myosin assembly or contractility, with implications for understanding cardiomyopathies and skeletal muscle diseases. Structural studies using recombinant MYL1 also aid in deciphering molecular mechanisms of myosin regulation and designing targeted therapies.
Overall, MYL1 recombinant protein is a vital tool for advancing muscle biology research and therapeutic development.
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