纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ATM |
Uniprot No | O43313 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-138aa |
氨基酸序列 | MTLHEPANSSASQSTDLCDFSGDLDPAPNPPHFPSHVVKATFAYISNCHK TKLKSILEILSKSPDSYQKILLAICEQAAETNNVYKKHRILKIYHLFVSL LLKDIKSGLGGAWAFVLRDVIYTLIHYINQRKLTIFSQ |
预测分子量 | 41 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ATM重组蛋白的3篇参考文献及其摘要概述:
1. **《Structural Basis of ATM Kinase Activation by Synergistic Substrate Recruitment》**
- 作者:Paull, T.T. 等(2017)
- 摘要:通过冷冻电镜技术解析了ATM激酶的三维结构,揭示了其通过MRE11复合物和底物协同招募的激活机制,为重组ATM蛋白在DNA损伤修复中的功能研究提供了结构基础。
2. **《Expression and Purification of Active ATM Protein Kinase from Human Cells》**
- 作者:Lee, J.H. 等(2015)
- 摘要:报道了一种高效表达和纯化活性重组人ATM蛋白的方法,验证其在体外对p53底物的磷酸化活性,为ATM功能研究和药物筛选提供了工具。
3. **《Functional Analysis of ATM Protein Kinase in DNA Double-Strand Break Repair》**
- 作者:Bakkenist, C.J. 等(2003)
- 摘要:利用重组ATM蛋白研究其在DNA双链断裂中的磷酸化调控网络,揭示ATM通过激活下游靶点(如CHK2)协调细胞周期检查点和修复机制。
这些文献涵盖了ATM重组蛋白的结构解析、表达纯化技术及功能机制研究,均为该领域的核心研究方向。
ATM (Ataxia-Telangiectasia Mutated) recombinant protein is derived from the ATM gene, which encodes a serine/threonine kinase critical for maintaining genomic stability. Mutations in ATM cause Ataxia-Telangiectasia (A-T), a rare autosomal recessive disorder characterized by neurodegeneration, immune dysfunction, and cancer predisposition. The ATM protein plays a central role in the DNA damage response (DDR), particularly in detecting and repairing double-strand breaks (DSBs). Upon DNA damage, ATM is activated via autophosphorylation and orchestrates cell cycle checkpoints, DNA repair, and apoptosis by phosphorylating downstream targets like CHK2. p53. and BRCA1.
Recombinant ATM protein is produced using biotechnological platforms (e.g., mammalian, insect, or bacterial expression systems) to enable functional and structural studies. Its large size (~370 kDa) and complex domain architecture (including a conserved PI3K-like kinase domain) pose challenges for recombinant expression, necessitating optimized purification strategies. Advances in structural biology, such as cryo-EM, have recently resolved ATM’s conformational dynamics, revealing mechanisms of activation and substrate recognition.
Researchers utilize recombinant ATM to dissect DDR pathways, model A-T pathophysiology, and screen therapeutic compounds. It also aids in studying ATM’s non-canonical roles in oxidative stress response, mitochondrial homeostasis, and insulin signaling. Despite progress, producing enzymatically active full-length ATM remains technically demanding, driving interest in truncated or modified variants for experimental or therapeutic applications. Ongoing research aims to leverage recombinant ATM for targeted cancer therapies, given its dual role as a tumor suppressor and a mediator of radiation resistance.
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