| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PRKAG2 |
| Uniprot No | Q9UGJ0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-328aa |
| 氨基酸序列 | MLEKLEFEDEAVEDSESGVYMRFMRSHKCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETWRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQNLDELGIGTYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALILTPAGAKQKETETE |
| 预测分子量 | 41.5 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3篇与PRKAG2重组蛋白相关的代表性文献摘要(内容为虚构示例，仅供参考格式)：
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1. **文献名称**：*Structural analysis of recombinant PRKAG2 protein reveals key domains for AMPK regulation*
**作者**：MacRae CA, et al.
**摘要**：本研究成功表达并纯化了人源PRKAG2重组蛋白，通过X射线晶体学解析其结构，发现其C端结构域对AMPK复合物的能量感知功能具有关键调控作用，为突变相关心肌病的机制提供了结构基础。
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2. **文献名称**：*Functional characterization of PRKAG2 mutations using recombinant proteins in cardiac disease models*
**作者**：Arad M, et al.
**摘要**：通过构建携带R302Q等致病突变的PRKAG2重组蛋白，在体外验证了突变体导致AMPK活性异常增强，并干扰心脏糖原代谢通路，阐明了遗传性预激综合征的分子机制。
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3. **文献名称**：*Recombinant PRKAG2 expression in E. coli: Optimization and enzymatic activity assays*
**作者**：Patel HH, et al.
**摘要**：开发了一种高效的大肠杆菌表达系统生产重组PRKAG2蛋白，优化纯化条件后获得高纯度产物，并通过体外ATP结合实验证实其参与AMPK能量感知的核心功能。
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(注：以上文献为示例性内容，实际引用需查阅PubMed等数据库获取真实发表论文。)
PRKAG2 recombinant protein is derived from the PRKAG2 gene, which encodes the gamma-2 regulatory subunit of adenosine monophosphate-activated protein kinase (AMPK), a critical energy sensor in eukaryotic cells. AMPK is a heterotrimeric complex comprising α, β, and γ subunits, with the γ subunit (including PRKAG2) playing a key role in binding adenosine nucleotides (AMP, ADP, ATP) to regulate kinase activity in response to cellular energy status. PRKAG2 mutations are linked to a rare autosomal dominant disorder called PRKAG2 syndrome, characterized by cardiac hypertrophy, conduction abnormalities (e.g., Wolff-Parkinson-White syndrome), and glycogen accumulation in cardiomyocytes.
Recombinant PRKAG2 protein is typically produced using expression systems (e.g., E. coli, mammalian cells) to study its structure-function relationships, interaction networks, and pathogenic mechanisms. Its production enables in vitro investigation of how mutations disrupt AMPK signaling, leading to metabolic dysregulation and cardiac pathologies. Researchers utilize this protein to analyze binding affinities for nucleotides, assess conformational changes, and screen potential therapeutic compounds targeting AMPK dysfunction. Structural studies, including X-ray crystallography and cryo-EM, have revealed critical domains involved in nucleotide sensing and subunit interactions. Additionally, PRKAG2 recombinant protein aids in developing cellular or animal models to mimic PRKAG2-associated diseases, facilitating mechanistic studies and preclinical trials. Its applications extend to diagnostics, where it serves as an antigen for antibody development to detect aberrant protein expression in clinical samples. Ongoing research focuses on leveraging this tool to design targeted therapies, such as gene-editing approaches or small molecules to restore AMPK homeostasis in metabolic and cardiovascular disorders.
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