纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | AOAH |
Uniprot No | P28039 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 35-575aa |
氨基酸序列 | LSNGHTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEKLFLKTTCYLVIDKFGSDIIKLLSADMNADVVCHTLEFCKQNTGQPLCHLYPLPKETWKFTLQKARQIVKKSPILKYSRSGSDICSLPVLAKICQKIKLAMEQSVPFKDVDSDKYSVFPTLRGYHWRGRDCNDSDESVYPGRRPNNWDVHQDSNCNGIWGVDPKDGVPYEKKFCEGSQPRGIILLGDSAGAHFHISPEWITASQMSLNSFINLPTALTNELDWPQLSGATGFLDSTVGIKEKSIYLRLWKRNHCNHRDYQNISRNGASSRNLKKFIESLSRNKVLDYPAIVIYAMIGNDVCSGKSDPVPAMTTPEKLYSNVMQTLKHLNSHLPNGSHVILYGLPDGTFLWDNLHNRYHPLGQLNKDMTYAQLYSFLNCLQVSPCHGWMSSNKTLRTLTSERAEQLSNTLKKIAASEKFTNFNLFYMDFAFHEIIQEWQKRGGQPWQLIEPVDGFHPNEVALLLLADHFWKKVQLQWPQILGKENPFNPQIKQVFGDQGGH |
预测分子量 | 62.4 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AOAH(Acyloxyacyl Hydrolase)重组蛋白的3篇参考文献示例,包含文献名称、作者及摘要概括:
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1. **文献名称**: *"Expression and Characterization of Recombinant Human AOAH in Mammalian Cells"*
**作者**: Smith J. et al.
**摘要**: 本研究成功在哺乳动物细胞(CHO细胞)中表达了重组人源AOAH蛋白,并通过亲和层析纯化获得高纯度产物。实验验证其酶活性可有效降解脂多糖(LPS)的毒性脂质A结构,为抗内毒素治疗研究提供了工具。
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2. **文献名称**: *"Bacterial Expression and Functional Analysis of AOAH in Sepsis Models"*
**作者**: Lee H. et al.
**摘要**: 作者利用大肠杆菌系统表达重组AOAH,优化表达条件后获得可溶性蛋白。动物实验表明,注射重组AOAH可显著降低败血症小鼠模型的炎症因子水平,提示其潜在临床应用价值。
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3. **文献名称**: *"Structural Insights into AOAH-Mediated LPS Detoxification"*
**作者**: Zhang Y. et al.
**摘要**: 通过X射线晶体学解析了重组AOAH的3D结构,揭示了其底物结合域的关键氨基酸残基。结合突变体实验,阐明了AOAH特异性水解LPS的分子机制,为设计新型抗炎药物奠定基础。
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注:以上文献为示例,实际引用时需根据具体研究通过学术数据库(如PubMed、Web of Science)检索最新或关键论文。
**Background of AOAH Recombinant Protein**
Acyloxyacyl hydrolase (AOAH) is a lipase enzyme primarily produced by macrophages and dendritic cells, playing a critical role in modifying bacterial lipopolysaccharides (LPS). LPS, a major component of the outer membrane of Gram-negative bacteria, triggers potent innate immune responses via Toll-like receptor 4 (TLR4). However, excessive or prolonged LPS exposure can lead to uncontrolled inflammation, contributing to sepsis, chronic inflammatory diseases, or immune paralysis. AOAH mitigates this by selectively cleaving secondary acyl chains from the lipid A moiety of LPS, converting it from a highly stimulatory endotoxin to a less inflammatory, "detoxified" form. This enzymatic activity is vital for resolving LPS-induced inflammation and restoring immune homeostasis.
Structurally, AOAH is a 70-kDa glycoprotein with a serine protease-like catalytic domain. Its recombinant form is engineered using expression systems such as mammalian cells (e.g., HEK293) or insect cells to ensure proper post-translational modifications, including glycosylation, which is essential for its stability and enzymatic function. Recombinant AOAH production involves cloning the AOAH gene into expression vectors, followed by purification via affinity chromatography.
Research on recombinant AOAH focuses on its therapeutic potential in sepsis, inflammatory bowel disease (IBD), and other conditions driven by dysregulated LPS responses. Preclinical studies demonstrate its ability to reduce hyperinflammation, accelerate bacterial clearance, and improve survival in sepsis models. Additionally, AOAH's role in metabolic endotoxemia and chronic inflammatory disorders highlights its broader clinical relevance. Challenges remain in optimizing its pharmacokinetics and delivery, but advances in protein engineering and targeted therapies may enhance its efficacy. Overall, recombinant AOAH represents a promising biologic to modulate LPS-driven pathologies, bridging innate immunity and inflammation resolution.
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