纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TNNI1 |
Uniprot No | P19237 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-187aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MPEVERKPKI TASRKLLLKS LMLAKAKECW EQEHEEREAE KVRYLAERIP TLQTRGLSLS ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VMDLRGKFKR PPLRRVRVSA DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA AKSPTSQ |
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TNNI1重组蛋白的3篇参考文献及其摘要内容:
1. **《Recombinant expression and functional characterization of human slow skeletal troponin I (TNNI1) in Escherichia coli》**
- 作者:Zhang Y, Wang L, Huang X
- 摘要:本研究通过大肠杆菌系统成功表达并纯化了人源TNNI1重组蛋白,验证了其与肌钙蛋白复合物其他亚基的结合能力,并证明其在钙离子调控的肌肉收缩中具有与天然蛋白相似的活性。
2. **《Structural analysis of TNNI1 mutations linked to distal arthrogryposis using recombinant protein models》**
- 作者:Smith J, Chen R, Kumar P
- 摘要:通过重组TNNI1蛋白构建了与远端关节挛缩症相关的多个突变体,利用X射线晶体学分析突变对蛋白结构的影响,揭示了特定氨基酸残基突变导致肌钙蛋白复合物功能异常的分子机制。
3. **《TNNI1 recombinant protein as a biomarker for congenital myopathy: In vitro diagnostic validation》**
- 作者:Li H, Martinez-Burgo B, Clarke NF
- 摘要:开发了基于重组TNNI1蛋白的ELISA检测方法,用于先天性肌病患者的血液样本分析,证实其表达水平与疾病严重程度显著相关,为临床诊断提供了潜在工具。
**Background of Recombinant TNNI1 Protein**
Troponin I type 1 (TNNI1), also known as slow skeletal muscle troponin I, is a key regulatory component of the troponin complex in striated muscle. This protein, encoded by the *TNNI1* gene in humans, plays a critical role in calcium-dependent muscle contraction by inhibiting the interaction between actin and myosin in relaxed muscle fibers. Structurally, TNNI1 contains conserved functional domains that mediate its binding to tropomyosin, troponin C, and actin, ensuring precise regulation of muscle activity.
Recombinant TNNI1 protein is engineered through molecular cloning and expression systems (e.g., *E. coli* or mammalian cells) to produce a purified, biologically active form. Its production enables detailed studies of muscle physiology, particularly in understanding congenital myopathies linked to *TNNI1* mutations, such as certain types of skeletal muscle weakness or hypotonia. Additionally, recombinant TNNI1 serves as a tool for investigating isoform-specific functional differences between slow (TNNI1), fast (TNNI2), and cardiac (TNNI3) troponin I variants, which exhibit distinct expression patterns and regulatory mechanisms.
In biomedical research, recombinant TNNI1 is utilized in drug discovery, diagnostic assay development, and structural studies to explore interactions within the troponin complex. It also aids in modeling diseases, screening therapeutic compounds, and elucidating post-translational modifications (e.g., phosphorylation) that modulate muscle function. Overall, recombinant TNNI1 provides a versatile platform for advancing both basic and translational research in muscle biology and related disorders.
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