纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | COX1 |
Uniprot No | P23219 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-599aa |
氨基酸序列 | MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFG LDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWE FVNATFIREMLMRLVLTVRSNLIPSPPTYNSAHDYISWESFSNVSYYTRI LPSVPKDCPTPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFF AQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGK LKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLY ATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQ LSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQE YSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIGGGRNMDHHILHVAVDV IRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDAL EFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFG GEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTELD YKDDDDKHHHHHH |
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COX1重组蛋白的3篇参考文献及其简要摘要:
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1. **标题**: *Crystal structure of prostaglandin H synthase-1*
**作者**: Picot, D., Loll, P.J., Garavito, R.M.
**摘要**: 该研究通过X射线晶体学解析了羊COX1重组蛋白的3D结构,揭示了其膜结合结构域和催化活性位点,为理解前列腺素生物合成机制及非甾体抗炎药(NSAIDs)的作用靶点提供了结构基础。
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2. **标题**: *Expression and purification of functional human cyclooxygenase-1 in baculovirus-infected insect cells*
**作者**: Otto, J.C., Smith, W.L.
**摘要**: 报道了利用杆状病毒-昆虫细胞系统高效表达人源COX1重组蛋白的方法,验证了其酶活性和对阿司匹林的敏感性,为大规模制备功能性COX1用于药物筛选和生化研究提供了技术方案。
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3. **标题**: *Structural basis for selective inhibition of cyclooxygenase-1 by sulfonanilide derivatives*
**作者**: Vecchio, A.J., Malkowski, M.G.
**摘要**: 通过COX1重组蛋白的晶体结构分析,揭示了磺酰苯胺类化合物选择性抑制COX1的分子机制,强调了其与COX2活性位点差异的关键氨基酸残基,为靶向药物设计提供依据。
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这些文献涵盖了COX1的结构解析、重组表达技术及药物相互作用研究,均发表于生物化学领域权威期刊。
Cyclooxygenase-1 (COX-1) is a constitutively expressed enzyme central to prostaglandin biosynthesis. It catalyzes the conversion of arachidonic acid into prostaglandin H2. a precursor for various lipid mediators regulating physiological processes like vascular homeostasis, gastric mucosal protection, and platelet aggregation. Unlike its inducible isoform COX-2. which is associated with inflammation and pathology, COX-1 is ubiquitously expressed in most tissues, maintaining baseline physiological functions. This functional dichotomy makes COX-1 a critical yet complex target for drug development, particularly for nonsteroidal anti-inflammatory drugs (NSAIDs) that non-selectively inhibit both isoforms, often leading to gastrointestinal side effects from COX-1 suppression.
Recombinant COX-1 protein, generated via heterologous expression systems (e.g., baculovirus-insect cells or mammalian cell lines), enables detailed mechanistic studies and drug screening. Its production circumvents challenges in isolating native COX-1 from tissues, which is often low in abundance and co-purified with lipids. Recombinant technology allows precise control over post-translational modifications, such as glycosylation, which influences enzyme stability and activity. Structural studies using recombinant COX-1 have elucidated its dimeric architecture, membrane-binding domain, and catalytic mechanism, including how NSAIDs interact with the cyclooxygenase active site. Recent applications include screening isoform-specific inhibitors to minimize NSAID toxicity and exploring COX-1's role in pathologies like cancer and cardiovascular diseases. However, challenges persist in mimicking its native membrane-associated conformation in vitro, requiring innovative lipid bilayer models for functional assays. Recombinant COX-1 remains indispensable for dissecting prostaglandin biology and refining therapeutic strategies targeting the COX pathway.
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