| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | COX2 |
| Uniprot No | P35354 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-604aa |
| 氨基酸序列 | MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFY GENCSTPEFLTRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAIMS YVLTSRSHLIDSPPTYNADYGYKSWEAFSNLSYYTRALPPVPDDCPTPLG VKGKKQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDH KRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKYQIIDGEMYPP TVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCD VLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPE LLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSIL LEHGITQFVESFTRQIAGRVAGGRNVPPAVQKVSQASIDQSRQMKYQSFN EYRKRFMLKPYESFEELTGEKEMSAELEALYGDIDAVELYPALLVEKPRP DAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGFQIINTASI QSLICNNVKGCPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKER STELDYKDDDDKHHHHHH |
| 预测分子量 | 71 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COX2重组蛋白的3篇代表性文献，包含标题、作者及摘要概括：
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1. **标题**：Structural Basis of Selective Inhibition of Cyclooxygenase-2 by Anti-Inflammatory Agents
**作者**：Kurumbail, R.G. 等(1996)
**摘要**：该研究通过X射线晶体学解析了重组COX-2蛋白的三维结构，揭示了其与COX-1的活性位点差异，解释了非甾体抗炎药(如塞来昔布)选择性抑制COX-2的分子机制。
2. **标题**：Expression and Selective Inhibition of the Constitutive and Inducible Forms of Human Cyclooxygenase
**作者**：Gierse, J.K. 等(1995)
**摘要**：研究成功在昆虫细胞中表达重组人COX-2蛋白，并开发了高效纯化方法，比较了COX-2与COX-1的酶动力学差异，验证了多种抑制剂的选择性作用。
3. **标题**：Characterization of Prostaglandin G/H Synthase 1 and 2 in Rat, Dog, Monkey, and Human Gastrointestinal Tracts
**作者**：Kargman, S. 等(1996)
**摘要**：通过重组COX-2蛋白表达，结合免疫组化分析，证实COX-2在炎症组织中高表达，而COX-1在正常组织中广泛存在，为靶向COX-2的抗炎药物研发提供了依据。
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以上文献聚焦于COX-2重组蛋白的结构解析、表达纯化及功能研究，均为该领域经典论文。如需更多文献或特定研究方向，可进一步补充说明。
**Background of COX-2 Recombinant Protein**
Cyclooxygenase-2 (COX-2), also known as prostaglandin-endoperoxide synthase 2 (PTGS2), is a key enzyme in the biosynthesis of prostaglandins, lipid mediators involved in inflammation, pain, and fever. Unlike its constitutively expressed isoform COX-1. COX-2 is primarily induced by proinflammatory stimuli, cytokines, or growth factors, making it a central therapeutic target for inflammatory diseases and cancer.
Recombinant COX-2 protein is engineered using molecular cloning techniques, often expressed in systems like *E. coli*, insect cells, or mammalian cells to ensure proper folding and enzymatic activity. This recombinant form retains the bifunctional cyclooxygenase and peroxidase activities of native COX-2. enabling researchers to study its structure-function relationships, inhibition mechanisms, and interactions with nonsteroidal anti-inflammatory drugs (NSAIDs) or selective COX-2 inhibitors (e.g., celecoxib).
COX-2’s role extends beyond inflammation; it is implicated in tumor progression, angiogenesis, and neurodegenerative disorders. Structural studies of recombinant COX-2 have revealed critical insights into its active site topology, particularly the larger hydrophobic pocket compared to COX-1. which explains the selectivity of certain inhibitors. Additionally, recombinant COX-2 is vital in drug discovery, serving as a target for screening anti-inflammatory or anticancer compounds.
Despite its utility, producing functional recombinant COX-2 remains challenging due to its membrane-associated nature and dependency on heme cofactors. Advances in purification strategies, such as affinity tagging and detergent solubilization, have improved yield and activity. Today, recombinant COX-2 is a cornerstone in both basic research and pharmaceutical development, bridging mechanistic biochemistry with therapeutic innovation.
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