| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CA7 |
| Uniprot No | P43166 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-264aa |
| 氨基酸序列 | MTGHHGWGYG QDDGPSHWHK LYPIAQGDRQ SPINIISSQA VYSPSLQPLE LSYEACMSLS ITNNGHSVQV DFNDSDDRTV VTGGPLEGPY RLKQFHFHWG KKHDVGSEHT VDGKSFPSEL HLVHWNAKKY STFGEAASAP DGLAVVGVFL ETGDEHPSMN RLTDALYMVR FKGTKAQFSC FNPKCLLPAS RHYWTYPGSL TTPPLSESVT WIVLREPICI SERQMGKFRS LLFTSEDDER IHMVNNFRPP QPLKGRVVKA SFRA |
| 预测分子量 | 29,6 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CA7重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
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1. **文献名称**：Expression and Purification of Recombinant Human Carbonic Anhydrase VII in E. coli
**作者**：Smith A, et al.
**摘要**：本研究报道了人源CA7基因在大肠杆菌中的高效表达及纯化策略，通过优化诱导条件和亲和层析技术获得高活性重组蛋白，并验证其酶动力学特性。
2. **文献名称**：Structural Insights into CA7 by X-ray Crystallography: Implications for Inhibitor Design
**作者**：Chen L, et al.
**摘要**：利用重组CA7蛋白进行晶体结构解析，揭示了其活性位点特征，为开发针对神经系统疾病的特异性抑制剂提供结构基础。
3. **文献名称**：Functional Role of Recombinant CA7 in pH Regulation of Glioblastoma Cells
**作者**：Wang Y, et al.
**摘要**：通过体外实验证明，重组CA7蛋白可调节胶质母细胞瘤细胞内pH平衡，抑制其迁移能力，提示CA7在癌症治疗中的潜在应用。
4. **文献名称**：Development of a CA7-Specific ELISA Kit Using Recombinant Protein Antigens
**作者**：Kim H, et al.
**摘要**：基于重组CA7蛋白建立高灵敏度ELISA检测方法，用于临床样本中CA7水平定量分析，助力相关生物标志物研究。
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注：以上文献为模拟内容，实际引用需查询真实数据库(如PubMed、Web of Science)。
Carbonic Anhydrase VII (CA7), a member of the carbonic anhydrase (CA) family, is a zinc-containing metalloenzyme that catalyzes the reversible hydration of carbon dioxide (CO₂) to bicarbonate (HCO₃⁻) and protons (H⁺). This enzyme plays a critical role in maintaining acid-base balance, ion transport, and cellular metabolism. CA7 is primarily expressed in the brain, kidneys, and salivary glands, with distinct tissue-specific functions. Unlike other CA isoforms (e.g., CA2 or CA9), CA7 is noted for its cytosolic localization and high catalytic efficiency, though its physiological roles remain less characterized compared to other isoforms. Dysregulation of CA7 has been implicated in neurological disorders, including epilepsy and Alzheimer’s disease, as well as certain cancers, suggesting its potential as a therapeutic target.
Recombinant CA7 protein is produced via genetic engineering, typically by expressing the human CA7 gene in bacterial (e.g., *E. coli*) or mammalian expression systems. This allows large-scale production of purified, bioactive CA7 for research and drug development. Recombinant CA7 retains enzymatic activity, enabling studies on its structure-function relationships, substrate specificity, and inhibition kinetics. It is widely used in biochemical assays, X-ray crystallography for structural analysis, and screening of CA inhibitors (CAIs) for therapeutic applications. Additionally, recombinant CA7 aids in exploring its role in disease mechanisms, such as pH regulation in tumor microenvironments or neuronal excitability modulation. Recent studies highlight its involvement in modulating oxidative stress and apoptosis pathways, expanding its relevance beyond traditional CA functions. As research progresses, recombinant CA7 continues to serve as a vital tool for elucidating isoform-specific biology and advancing targeted therapies.
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