纯度 | > 95 % SDS-PAGE. |
种属 | Human |
靶点 | CA2 |
Uniprot No | P00918 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-260aa |
氨基酸序列 | MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK |
预测分子量 | 30.7kDa |
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CA2(碳酸酐酶II)重组蛋白研究的模拟参考文献示例,供参考(注:文献为模拟示例,实际文献需通过学术数据库检索确认):
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1. **文献名称**: *Expression and purification of recombinant human carbonic anhydrase II in Escherichia coli*
**作者**: Smith JL, et al.
**摘要**: 本研究利用大肠杆菌表达系统成功表达并纯化重组人碳酸酐酶II(rhCA2),通过亲和层析获得高纯度蛋白,并验证其酶活性与天然蛋白一致。
2. **文献名称**: *Crystal structure analysis of recombinant CA2 reveals pH-dependent conformational changes*
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析重组CA2的三维结构,揭示其在不同pH条件下的构象变化,为设计靶向CA2的抑制剂提供结构基础。
3. **文献名称**: *Functional characterization of recombinant CA2 in a zebrafish model of osteoporosis*
**作者**: Wang H, et al.
**摘要**: 在斑马鱼骨质疏松模型中,重组CA2的过表达显著影响骨矿物质代谢,提示其在骨骼疾病治疗中的潜在应用价值。
4. **文献名称**: *Development of a high-throughput screening assay for CA2 inhibitors using recombinant protein*
**作者**: Müller R, et al.
**摘要**: 基于重组CA2蛋白建立高通量筛选平台,成功鉴定多个新型CA2抑制剂,为抗青光眼药物研发提供候选分子。
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建议通过PubMed、Web of Science或Google Scholar检索关键词(如“recombinant CA2 protein”、“carbonic anhydrase II expression”)获取真实文献。
Carbonic anhydrase II (CA2), a member of the carbonic anhydrase (CA) enzyme family, is a zinc-containing metalloenzyme critical for regulating pH homeostasis and gas exchange in biological systems. It catalyzes the reversible hydration of carbon dioxide (CO₂) to bicarbonate (HCO₃⁻) and protons (H⁺), a reaction essential for processes such as respiration, bone resorption, renal acid secretion, and cerebrospinal fluid production. Among the 15 human CA isoforms, CA2 is one of the most well-characterized due to its high catalytic efficiency, ubiquitous tissue distribution, and involvement in genetic disorders like osteopetrosis and renal tubular acidosis.
Recombinant CA2 protein is produced via genetic engineering, typically by expressing the human CA2 gene in bacterial (e.g., *E. coli*), yeast, or mammalian cell systems. This allows large-scale production of the enzyme with high purity and activity. Recombinant CA2 retains the native structure and function, making it invaluable for biomedical research and industrial applications. In drug discovery, it serves as a target for developing inhibitors to treat glaucoma, epilepsy, and altitude sickness. Its role in CO₂ metabolism has also spurred interest in carbon capture technologies.
Structurally, recombinant CA2 facilitates studies on enzyme kinetics, inhibitor binding, and metal ion coordination. Crystallographic analyses using recombinant protein have revealed details of its active site and catalytic mechanism. Challenges in production include maintaining proper zinc incorporation and avoiding aggregation during purification. Advances in expression systems and purification techniques continue to enhance its utility in both basic research and biotechnological innovations.
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