| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATP4a |
| Uniprot No | P20648 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 350-783aa |
| 氨基酸序列 | TVTVCLSLTAKRLASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYRDRFPKVCEIPFNSTNKFQLSIHTLEDPRDPRHLLVMKGAPERVLERCSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYAFDVEAMNFPSSGLCFAGLVSMIDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDNL |
| 预测分子量 | 54.6 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ATP4a重组蛋白的3篇参考文献及其摘要内容：
1. **"Functional characterization of recombinant ATP4a in gastric proton secretion"**
*作者：Sachs G. et al.*
摘要：研究利用昆虫细胞系统表达重组ATP4a蛋白，验证其作为H+/K+-ATP酶核心亚基的功能，证实其在胃酸分泌中的关键作用及对抑制剂奥美拉唑的敏感性。
2. **"Cryo-EM structure of the gastric H+/K+-ATPase with bound potassium ions"**
*作者：Abe K. et al.*
摘要：通过冷冻电镜解析ATP4a重组蛋白的分子结构，揭示其与钾离子结合的构象变化机制，为理解质子泵的离子转运提供结构基础。
3. **"ATP4a knockout mice exhibit impaired acid secretion and mucosal defects"**
*作者：Judith A. et al.*
摘要：利用基因编辑技术构建ATP4a缺陷小鼠模型，发现其胃酸分泌显著减少，并伴随胃黏膜萎缩，证明该蛋白在维持胃生理功能中的必要性。
4. **"Recombinant ATP4a-based high-throughput screening for acid suppression drugs"**
*作者：Munson K. et al.*
摘要：开发基于重组ATP4a蛋白的药物筛选平台，成功鉴定新型质子泵抑制剂，为胃酸相关疾病治疗提供潜在候选化合物。
(注：以上为模拟文献，实际引用时需核实具体文献信息。)
ATP4a, also known as the alpha subunit of the gastric H+/K+ ATPase, is a critical enzyme responsible for acid secretion in the parietal cells of the stomach. As a member of the P-type ATPase family, it functions as an ion pump that exchanges cytoplasmic protons (H+) for luminal potassium ions (K+), generating the highly acidic environment necessary for digestion and microbial defense. This transmembrane protein consists of a catalytic α-subunit (ATP4a) and a regulatory β-subunit (ATP4b), forming a heterodimeric complex essential for its activity.
The recombinant ATP4a protein is engineered through molecular cloning and expression in heterologous systems like mammalian cells (e.g., HEK293) or insect cells (e.g., baculovirus systems) to study its structure, function, and interactions. Purification typically involves affinity chromatography tags (e.g., His-tag) for isolation. Recombinant ATP4a retains key structural features, including ten transmembrane domains, phosphorylation sites, and ATP-binding motifs, enabling researchers to investigate its enzymatic kinetics, ion transport mechanisms, and regulation under physiological or pathological conditions.
Dysregulation of ATP4a is linked to gastric acid-related disorders such as peptic ulcers, gastroesophageal reflux disease (GERD), and Zollinger-Ellison syndrome. It is a primary target for proton pump inhibitors (PPIs) like omeprazole, which irreversibly inhibit acid secretion. Recombinant ATP4a facilitates drug discovery by serving as a platform for screening novel acid-suppressive therapies or studying resistance mechanisms. Additionally, it aids in structural studies (e.g., cryo-EM) to resolve conformational changes during the catalytic cycle and supports antibody development for diagnostic applications. Its recombinant form has become indispensable for advancing both basic research and therapeutic innovations in gastroenterology.
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