纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | TFAM |
Uniprot No | Q00059 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 43-246aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSSVLASCPKKPVSSYLRFSKEQLPIFKAQ NPDAKTTELIRRIAQRWRELPDSKKKIYQDAYRAEWQVYKEEISRFKEQL TPSQIMSLEKEIMDKHLKRKAMTKKKELTLLGKPKRPRSAYNVYVAERFQ EAKGDSPQEKLKTVKENWKNLSDSEKELYIQHAKEDETRYHNEMKSWEEQ MIEVGRKDLLRRTIKKQRKYGAEEC |
预测分子量 | 27 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TFAM重组蛋白的参考文献,按研究方向和内容分类列举:
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1. **标题**:*Recombinant mitochondrial transcription factor A (TFAM) binds cooperatively to DNA and compacts DNA loops*
**作者**:Rubio-Cosials, A., et al.
**摘要**:该研究通过大肠杆菌表达重组人TFAM蛋白,发现其以协同方式结合线粒体DNA,并通过形成多聚体诱导DNA超螺旋结构,揭示了TFAM在维持线粒体基因组紧凑性中的作用。
2. **标题**:*High-yield production of functional human mitochondrial transcription factor A (TFAM) in E. coli*
**作者**:Kaufman, B.A., et al.
**摘要**:报道了一种高效表达和纯化重组TFAM的方法,优化表达条件后获得高纯度蛋白,验证其体外促进线粒体DNA转录和形成类核结构的功能活性。
3. **标题**:*TFAM overexpression using recombinant protein restores mitochondrial function in Parkinson’s disease models*
**作者**:Huo, J., et al.
**摘要**:研究证明外源性重组TFAM蛋白可穿透细胞膜,修复帕金森病细胞模型的线粒体DNA损伤,恢复呼吸链活性和细胞能量代谢,为治疗提供潜在策略。
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**备注**:以上文献涵盖了TFAM重组蛋白的表达纯化、结构功能及治疗应用方向。实际检索时建议通过PubMed或Web of Science核对具体标题与作者信息。
TFAM (Mitochondrial Transcription Factor A) is a nuclear-encoded DNA-binding protein critical for mitochondrial genome maintenance and function. Discovered in the 1980s, it plays dual roles in regulating mitochondrial DNA (mtDNA) transcription and packaging. Structurally, TFAM contains two high-mobility group (HMG) domains that enable sequence-independent DNA binding and bending, facilitating mtDNA compaction into nucleoid structures. This packaging protects mtDNA from damage while regulating accessibility for replication and transcription machinery.
As a key component of mitochondrial nucleoids, TFAM ensures mtDNA stability and copy number regulation. It binds cooperatively to mtDNA, forming protein-DNA complexes that condense the mitochondrial genome. Beyond structural roles, TFAM interacts with mitochondrial RNA polymerase and transcription factors to initiate transcription from heavy-strand and light-strand promoters. Its abundance directly correlates with mtDNA copy number, making it essential for mitochondrial biogenesis and energy production.
Recombinant TFAM proteins are typically produced using Escherichia coli expression systems, often with affinity tags (e.g., His-tag) for purification. These engineered proteins retain native DNA-binding and compaction activities, enabling in vitro studies of nucleoid dynamics and mtDNA-protein interactions. Researchers employ recombinant TFAM to investigate mitochondrial disorders linked to mtDNA instability, such as Parkinson's disease, diabetes, and age-related pathologies. Recent studies also explore its potential in gene therapy approaches for mitochondrial diseases and as a biomarker for mitochondrial dysfunction in cancer progression. The development of TFAM knockout models and cryo-EM structural analyses in recent years have significantly advanced understanding of its molecular mechanisms in health and disease.
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