纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ATP1a2 |
Uniprot No | P50993 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-1020aa |
氨基酸序列 | MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDVLARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVIREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSTILVQGKEIPLDKEMQDAFQNAYMELGGLGERVLGFCQLNLPSGKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPMSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNSQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRTMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY |
预测分子量 | 112,2 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ATP1a2重组蛋白的3条参考文献示例(注:内容为模拟生成,非真实文献):
1. **文献名称**:Functional characterization of recombinant ATP1a2 in a mammalian expression system
**作者**:Smith A, et al.
**摘要**:本研究成功在HEK293细胞中表达并纯化ATP1a2重组蛋白,证实其具有钠钾ATP酶活性,并通过电生理实验揭示了其对离子转运的调控机制。
2. **文献名称**:Structural insights into ATP1a2 mutations linked to familial hemiplegic migraine
**作者**:Chen L, et al.
**摘要**:通过冷冻电镜解析ATP1a2重组蛋白的突变体结构,发现特定突变导致蛋白构象变化,影响离子泵功能,为偏瘫型偏头痛的致病机制提供分子基础。
3. **文献名称**:ATP1a2 recombinant protein expression in insect cells and its role in astrocyte function
**作者**:Wang Y, et al.
**摘要**:利用杆状病毒-昆虫细胞系统高效表达ATP1a2重组蛋白,证明其在星形胶质细胞中参与细胞外钾离子清除,并验证其与癫痫模型的关联性。
如需真实文献,建议通过PubMed或Google Scholar以关键词“ATP1a2 recombinant protein”或“ATP1A2 expression”检索。
**Background of ATP1A2 Recombinant Protein**
ATP1A2. a member of the P-type ATPase family, encodes the α2 subunit of the sodium-potassium ATPase (Na+/K+-ATPase), an essential transmembrane protein responsible for maintaining electrochemical gradients across cell membranes. This enzyme actively transports three sodium ions out of the cell and two potassium ions into the cell per ATP hydrolyzed, crucial for cellular homeostasis, neuronal excitability, and secondary transport processes. The α2 subunit is predominantly expressed in astrocytes, cardiac muscle, and skeletal muscle, where it plays specialized roles in ion balance and signaling.
Mutations in the *ATP1A2* gene are linked to familial hemiplegic migraine type 2 (FHM2) and other neurological disorders, including epilepsy and alternating hemiplegia. These mutations impair ion transport, leading to disrupted glutamate clearance, cortical spreading depolarization, and altered neuronal activity. Recombinant ATP1A2 protein is engineered to study these mechanisms, enabling in vitro analysis of wild-type and mutant isoforms.
Produced via heterologous expression systems (e.g., mammalian cells or insect cells), recombinant ATP1A2 retains post-translational modifications critical for its function. It is utilized for structural studies (e.g., cryo-EM), drug screening, and functional assays to evaluate ion transport kinetics or pathogenicity of mutations. Additionally, it serves as a tool for developing therapeutic strategies targeting Na+/K+-ATPase dysfunction. Research on recombinant ATP1A2 enhances understanding of its physiological roles and contributions to disease, offering potential pathways for precision medicine in neurological and cardiovascular disorders.
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