| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | 15-LO-2 |
| Uniprot No | O15296 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-676aa |
| 氨基酸序列 | MAEFRVRVSTGEAFGAGTWDKVSVSIVGTRGESPPLPLDNLGKEFTAGAE EDFQVTLPEDVGRVLLLRVHKAPPVLPLLGPLAPDAWFCRWFQLTPPRGG HLLFPCYQWLEGAGTLVLQEGTAKVSWADHHPVLQQQRQEELQARQEMYQ WKAYNPGWPHCLDEKTVEDLELNIKYSTAKNANFYLQAGSAFAEMKIKGL LDRKGLWRSLNEMKRIFNFRRTPAAEHAFEHWQEDAFFASQFLNGLNPVL IRRCHYLPKNFPVTDAMVASVLGPGTSLQAELEKGSLFLVDHGILSGIQT NVINGKPQFSAAPMTLLYQSPGCGPLLPLAIQLSQTPGPNSPIFLPTDDK WDWLLAKTWVRNAEFSFHEALTHLLHSHLLPEVFTLATLRQLPHCHPLFK LLIPHTRYTLHINTLARELLIVPGQVVDRSTGIGIEGFSELIQRNMKQLN YSLLCLPEDIRTRGVEDIPGYYYRDDGMQIWGAVERFVSEIIGIYYPSDE SVQDDRELQAWVREIFSKGFLNQESSGIPSSLETREALVQYVTMVIFTCS AKHAAVSAGQFDSCAWMPNLPPSMQLPPPTSKGLATCEGFIATLPPVNAT CDVILALWLLSKEPGDQRPLGTYPDEHFTEEAPRRSIATFQSRLAQISRG IQERNRGLVLPYTYLDPPLIENSVSI |
| 预测分子量 | 102 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3篇关于15-LO-2重组蛋白的模拟参考文献示例(注：文献为虚构，仅供格式参考)：
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1. **文献名称**: *"Expression and Characterization of Recombinant Human 15-Lipoxygenase-2 in Baculovirus-Insect Cell System"*
**作者**: Johnson, R. et al.
**摘要**: 研究利用杆状病毒-昆虫细胞系统高效表达15-LO-2重组蛋白，通过亲和层析纯化获得高纯度蛋白，并证实其催化花生四烯酸生成15-HETE的酶活性，为体外酶学研究提供可靠工具。
2. **文献名称**: *"Structural Insights into 15-LO-2 Substrate Selectivity via Site-Directed Mutagenesis"*
**作者**: Chen, L. & Wang, H.
**摘要**: 通过定点突变技术分析15-LO-2重组蛋白的底物结合域，发现关键氨基酸残基(如His538)对其氧化特定多不饱和脂肪酸(如DHA)的选择性起决定性作用。
3. **文献名称**: *"Recombinant 15-LO-2 Modulates Macrophage Lipid Metabolism in Atherosclerosis Models"*
**作者**: Martinez, S. et al.
**摘要**: 研究重组15-LO-2蛋白对巨噬细胞脂质代谢的调控作用，发现其过表达促进氧化脂质生成并加剧动脉粥样硬化斑块炎症反应，提示潜在治疗靶点。
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**建议**：实际文献可通过PubMed或Google Scholar搜索关键词“15-LOX-2 recombinant”“human 15-lipoxygenase-2 expression”获取。部分经典文献可能涉及该蛋白的克隆、酶学特性或疾病关联机制。
15-Lipoxygenase-2 (15-LO-2), also known as ALOX15B, is a member of the lipoxygenase (LOX) enzyme family that catalyzes the dioxygenation of polyunsaturated fatty acids (PUFAs) into bioactive lipid mediators. Initially identified in the 1990s, 15-LO-2 shares structural homology with other LOX isoforms but exhibits distinct substrate preferences and tissue-specific expression. It primarily oxygenates arachidonic acid and linoleic acid to generate 15(S)-hydroperoxyeicosatetraenoic acid (15(S)-HpETE) and 13(S)-hydroxyoctadecadienoic acid (13(S)-HODE), respectively, which regulate inflammatory responses, cell proliferation, and apoptosis.
Expressed predominantly in epithelial tissues, including the prostate, skin, and cornea, 15-LO-2 has been implicated in both physiological and pathological processes. Unlike its paralog 15-LO-1 (ALOX15), which is linked to pro-inflammatory pathways, 15-LO-2 displays context-dependent roles. Studies suggest it may act as a tumor suppressor in prostate cancer by promoting oxidative stress-induced cell death, yet its overexpression in certain cancers correlates with poor prognosis, indicating dual functionalities.
Recombinant 15-LO-2 protein is typically produced in bacterial (e.g., E. coli) or eukaryotic (e.g., insect cell) systems to enable structural and functional studies. Purified recombinant 15-LO-2 retains catalytic activity and is used to investigate enzyme kinetics, substrate specificity, and inhibitor screening. Its crystal structure reveals a conserved LOX fold with a catalytic non-heme iron center, though unique loop regions may explain isoform-specific behaviors.
Research on recombinant 15-LO-2 continues to explore its therapeutic potential, particularly in modulating lipid-mediated signaling in inflammation and cancer. However, its precise biological roles and regulatory mechanisms remain partially unresolved, necessitating further mechanistic studies.
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