| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNNI2 |
| Uniprot No | P48788 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-182aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGDEEKRNRAITARRQHLKSVMLQIAATEL EKEESRREAEKQNYLAEHCPPLHIPGSMSEVQELCKQLHAKIDAAEEEKY DMEVRVQKTSKELEDMNQKLFDLRGKFKRPPLRRVRMSADAMLKALLGSK HKVCMDLRANLKQVKKEDTEKERDLRDVGDWRKNIEEKSGMEGRKKMFES ES |
| 预测分子量 | 24 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TNNI2重组蛋白的3篇参考文献示例(文献信息为模拟内容，实际需根据具体研究补充)：
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1. **文献名称**: *Expression and Functional Analysis of Recombinant Human TNNI2 in a Muscular Disorder Model*
**作者**: Smith A, et al.
**摘要**: 本研究通过大肠杆菌系统成功表达并纯化了重组人源TNNI2蛋白，并验证其在体外对钙离子敏感性的调节功能。实验发现，TNNI2突变体(如R174Q)会导致肌钙蛋白复合体稳定性下降，揭示了其在远端关节弯曲症(DA)中的致病机制。
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2. **文献名称**: *Structural Characterization of Recombinant TNNI2 Using X-ray Crystallography*
**作者**: Chen L, et al.
**摘要**: 通过X射线晶体学解析了重组TNNI2蛋白的高分辨率三维结构，揭示了其与肌钙蛋白T(TNNT3)的关键结合域。该结构为开发靶向TNNI2的分子药物提供了理论基础。
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3. **文献名称**: *Recombinant TNNI2 as a Biomarker for Early Diagnosis of Congenital Myopathies*
**作者**: Kim H, et al.
**摘要**: 研究利用重组TNNI2蛋白开发了一种新型ELISA检测方法，用于定量患者血清中TNNI2水平。临床数据显示，TNNI2表达异常与先天性肌病严重程度显著相关，表明其作为诊断标志物的潜力。
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如需实际文献，建议通过PubMed或Google Scholar检索关键词 **"TNNI2 recombinant protein"** 或 **"TNNI2 expression"**，并筛选涉及重组表达、功能研究或疾病应用的论文。
**Background of TNNI2 Recombinant Protein**
Troponin I type 2 (TNNI2), a skeletal muscle-specific isoform of the troponin I family, is a critical regulatory component of the troponin complex in striated muscles. This complex, composed of troponin I (TnI), troponin T (TnT), and troponin C (TnC), regulates calcium-dependent skeletal muscle contraction by modulating interactions between actin and myosin filaments. TNNI2 is predominantly expressed in fast-twitch muscle fibers and plays a vital role in maintaining muscle function and contractile dynamics.
The recombinant TNNI2 protein is engineered using molecular cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. Its production enables detailed biochemical studies, including structural analyses, interaction assays, and functional investigations into muscle regulation. Researchers utilize recombinant TNNI2 to explore its role in neuromuscular disorders, such as distal arthrogryposis (DA), where mutations in *TNNI2* are linked to congenital contractures and impaired muscle development.
Beyond basic research, recombinant TNNI2 serves as a tool for diagnostic applications, including antibody validation and biomarker discovery. It also holds therapeutic potential, particularly in gene therapy or drug screening for muscle-related diseases. Recent studies highlight its involvement in signaling pathways that influence muscle regeneration and atrophy, making it a focal point in developing treatments for muscular dystrophies or age-related sarcopenia.
Overall, TNNI2 recombinant protein bridges molecular insights with clinical applications, offering a versatile platform to advance understanding of muscle physiology and pathology.
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