| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MYBPC2 |
| Uniprot No | Q14324 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 739-1141aa |
| 氨基酸序列 | EPLHLIVEDVTDTTTTLKWRPPNRIGAGGIDGYLVEYCLEGSEEWVPANTEPVERCGFTVKNLPTGARILFRVVGVNIAGRSEPATLAQPVTIREIAEPPKIRLPRHLRQTYIRKVGEQLNLVVPFQGKPRPQVVWTKGGAPLDTSRVHVRTSDFDTVFFVRQAARSDSGEYELSVQIENMKDTATIRIRVVEKAGPPINVMVKEVWGTNALVEWQAPKDDGNSEIMGYFVQKADKKTMEWFNVYERNRHTSCTVSDLIVGNEYYFRVYTENICGLSDSPGVSKNTARILKTGITFKPFEYKEHDFRMAPKFLTPLIDRVVVAGYSAALNCAVRGHPKPKVVWMKNKMEIREDPKFLITNYQGVLTLNIRRPSPFDAGTYTCRAVNELGEALAECKLEVRVPQ |
| 预测分子量 | 47.5 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MYBPC2重组蛋白的假设性参考文献示例(请注意文献信息为模拟生成，建议通过学术数据库核实真实文献)：
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1. **标题**：Expression and Purification of Recombinant MYBPC2 in *E. coli* for Functional Studies
**作者**：Smith A, et al. (2020)
**摘要**：研究报道了在大肠杆菌中高效表达带有His标签的重组MYBPC2蛋白的优化方法，通过亲和层析纯化并验证其结构完整性，为后续功能研究提供基础。
2. **标题**：Structural Insights into MYBPC2’s Role in Myosin Binding via Cryo-EM Analysis
**作者**：Johnson L, et al. (2018)
**摘要**：利用冷冻电镜解析重组MYBPC2的C端结构域与肌球蛋白复合体的三维结构，揭示其调控肌肉收缩的分子机制及与遗传性心肌病的潜在关联。
3. **标题**：Functional Characterization of MYBPC2 Mutants Using Recombinant Protein Assays
**作者**：Lee S, et al. (2021)
**摘要**：通过体外结合实验比较野生型与突变型重组MYBPC2蛋白，发现特定突变削弱其与肌球蛋白的结合能力，提示其在肥厚型心肌病中的致病机制。
4. **标题**：High-Throughput Drug Screening Targeting Recombinant MYBPC2 for Cardiomyopathy Therapy
**作者**：Brown K, et al. (2022)
**摘要**：建立基于重组MYBPC2蛋白的药物筛选平台，鉴定出可增强其稳定性的化合物，为开发心肌病治疗策略提供潜在候选分子。
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**建议**：使用关键词“MYBPC2 recombinant”、“MYBPC2 expression”或“MYBPC2 structure”在PubMed、Google Scholar等平台检索真实文献。
MYBPC2. or Myosin Binding Protein C2. is a member of the myosin-binding protein C (MyBPC) family, which plays critical roles in the structural organization and functional regulation of striated muscle. While MYBPC1 and MYBPC3 are predominantly expressed in skeletal and cardiac muscle, respectively, MYBPC2 is primarily found in fast-twitch skeletal muscle fibers, though its expression patterns and physiological roles remain less characterized compared to other isoforms. This protein is encoded by the MYBPC2 gene in humans and is composed of immunoglobulin (Ig) and fibronectin type III (FnIII) domains, which mediate interactions with myosin heavy chains, actin, and titin. These interactions contribute to the assembly and stability of sarcomeres, the basic contractile units of muscle cells, and modulate cross-bridge cycling during muscle contraction.
Recombinant MYBPC2 protein is engineered through molecular cloning and heterologous expression systems (e.g., bacterial, insect, or mammalian cells) to study its biochemical properties, structural dynamics, and functional interactions. Researchers utilize purified recombinant MYBPC2 to investigate its role in muscle development, contractility, and disease mechanisms. For instance, mutations in MYBPC3 are linked to hypertrophic cardiomyopathy, but MYBPC2’s association with skeletal muscle disorders, such as myopathies or muscular dystrophies, is an emerging area of interest. Recombinant protein technology enables in vitro studies, including binding assays, structural analyses (e.g., X-ray crystallography, cryo-EM), and drug screening for potential therapeutics targeting MYBPC2-related pathologies.
Despite its significance, MYBPC2 remains understudied relative to other isoforms. Recombinant MYBPC2 provides a tool to address knowledge gaps, particularly its regulatory mechanisms in fast-twitch muscle physiology and its potential cross-talk with signaling pathways. Ongoing research aims to clarify its contributions to muscle adaptation, exercise response, and disease, leveraging recombinant protein-based approaches to unravel its multifunctional roles in health and disease.
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