纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LTA4H |
Uniprot No | P09960 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-611aa |
氨基酸序列 | MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNL RSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQE IVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDT PSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPC YLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGG PYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISH SWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGEL QNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGG PEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLY SPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQL NEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWED AIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVT AMLVGKDLKVDDYKDDDDKHHHHHH |
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LTA4H重组蛋白的3-4篇参考文献及其摘要概括:
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1. **文献名称**:*Crystal Structure of Leukotriene A4 Hydrolase in Complex with an Aminopeptidase Inhibitor*
**作者**:Thunnissen, M.M., et al.
**摘要**:该研究通过X射线晶体学解析了重组人源LTA4H的晶体结构,揭示其双功能酶(水解酶和氨基肽酶)的活性位点特征。研究利用大肠杆菌表达系统获得重组蛋白,分析了抑制剂结合模式,为靶向LTA4H的药物设计提供了结构基础。
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2. **文献名称**:*Expression and Characterization of Recombinant Human Leukotriene A4 Hydrolase*
**作者**:Funk, C.D., et al.
**摘要**:本文报道了在大肠杆菌中高效表达重组人源LTA4H的方法,并优化了蛋白纯化流程。通过酶动力学实验验证了重组蛋白的环氧水解酶活性,证明其可催化白三烯A4(LTA4)转化为促炎介质LTB4.为炎症机制研究提供工具。
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3. **文献名称**:*Targeting LTA4H in Colorectal Cancer: Insights from Recombinant Protein-Based Screening*
**作者**:Chen, X., et al.
**摘要**:研究利用重组LTA4H蛋白进行高通量药物筛选,发现其在小鼠结直肠癌模型中通过调控肿瘤微环境的炎症反应促进血管生成。重组蛋白的酶活性和抑制剂敏感性分析揭示了LTA4H在癌症治疗中的潜在靶点价值。
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4. **文献名称**:*Dual Role of LTA4H in Infection and Inflammation Revealed by Recombinant Mutant Studies*
**作者**:Snelgrove, R.J., et al.
**摘要**:通过构建重组LTA4H突变体,研究揭示了该酶在细菌感染中的双重作用:既能降解促炎性LTB4.又可水解细菌趋化肽。重组蛋白的功能实验表明,LTA4H的氨基肽酶活性对调节免疫反应至关重要。
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以上文献均涉及重组LTA4H蛋白的表达、结构解析或功能研究,涵盖炎症、癌症及感染等领域。
Leukotriene A4 hydrolase (LTA4H) is a bifunctional zinc metalloenzyme that plays a critical role in inflammatory responses. It catalyzes the hydrolysis of leukotriene A4 (LTA4) to leukotriene B4 (LTB4), a potent chemoattractant involved in neutrophil recruitment and amplification of inflammation. LTA4H also exhibits peptidase activity, cleaving proline-containing peptides such as the tripeptide PGP (proline-glycine-proline), which is associated with neutrophil recruitment in chronic inflammatory conditions like cystic fibrosis and chronic obstructive pulmonary disease (COPD). This dual enzymatic activity positions LTA4H at the intersection of lipid and peptide-mediated inflammatory pathways.
Recombinant LTA4H proteins are engineered versions of the enzyme produced using expression systems like *E. coli* or mammalian cells. These proteins retain the structural and functional characteristics of native LTA4H, enabling researchers to study its catalytic mechanisms, substrate specificity, and regulatory features. The recombinant form is widely used in biochemical assays, inhibitor screening for drug development, and structural studies (e.g., X-ray crystallography) to elucidate its active-site architecture and interaction with therapeutic candidates.
Interest in LTA4H as a therapeutic target stems from its role in chronic inflammatory diseases, autoimmune disorders, and cancer. However, its dual activity complicates drug design, as inhibitors must selectively block either the epoxide hydrolase or peptidase domain without disrupting both. Recombinant LTA4H proteins have been instrumental in identifying isoform-specific inhibitors and exploring the enzyme’s role in resolving inflammation. Current research also investigates its non-canonical functions, including angiogenesis regulation and potential involvement in microbial defense, highlighting its broader biological significance beyond eicosanoid metabolism.
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