| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HAAO |
| Uniprot No | P46952 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-286aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMERRLG VRAWVKENRG SFQPPVCNKL MHQEQLKVMF IGGPNTRKDY HIEEGEEVFY QLEGDMVLRV LEQGKHRDVV IRQGEIFLLP ARVPHSPQRF ANTVGLVVER RRLETELDGL RYYVGDTMDV LFEKWFYCKD LGTQLAPIIQ EFFSSEQYRT GKPIPDQLLK EPPFPLSTRS IMEPMSLDAW LDSHHRELQA GTPLSLFGDT YETQVIAYGQ GSSEGLRQNV DVWLWQLEGS SVVTMGGRRL SLAPDDSLLV LAGTSYAWER TQGSVALSVT QDPACKKPLG |
| 预测分子量 | 35 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HAAO(3-羟基邻氨基苯甲酸3.4-双加氧酶)重组蛋白的3篇参考文献摘要示例(文献名称与作者为虚构，仅供示例参考)：
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1. **文献名称**：*Expression and Purification of Recombinant HAAO in Escherichia coli for Structural Studies*
**作者**：Smith J, et al.
**摘要**：本研究报道了HAAO基因在大肠杆菌中的重组表达及纯化方法，利用His标签亲和层析获得高纯度蛋白。通过圆二色谱分析证实其二级结构完整性，并测定其催化活性，为后续酶学机制研究提供基础。
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2. **文献名称**：*Crystal Structure of Human HAAO Reveals Insights into Substrate Binding*
**作者**：Lee S, et al.
**摘要**：通过重组表达人源HAAO蛋白，结合X射线晶体学解析其三维结构(分辨率2.1 Å)，揭示了3-羟基邻氨基苯甲酸底物结合的关键氨基酸残基，阐明了其催化双加氧反应的分子机制。
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3. **文献名称**：*Functional Characterization of Recombinant HAAO in Neuroinflammatory Pathways*
**作者**：Zhang Y, et al.
**摘要**：研究利用哺乳动物细胞表达系统制备重组HAAO蛋白，发现其催化产物喹啉酸可激活小胶质细胞炎症信号通路，提示HAAO在神经退行性疾病中的潜在作用。
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**备注**：以上文献为模拟示例，实际研究中建议通过PubMed或Web of Science检索真实文献(关键词：HAAO, recombinant, 3-hydroxyanthranilic acid dioxygenase)。
**Background of HAAO Recombinant Protein**
3-Hydroxyanthranilic acid 3.4-dioxygenase (HAAO) is a key enzyme in the kynurenine pathway, a major route of tryptophan metabolism in mammals. It catalyzes the conversion of 3-hydroxyanthranilic acid (3-HAA) into 2-amino-3-carboxymuconic semialdehyde (ACMS), a reaction critical for the de novo synthesis of quinolinic acid (QUIN). QUIN serves as a precursor for nicotinamide adenine dinucleotide (NAD+) biosynthesis and acts as a neuroactive metabolite, influencing glutamate receptor activity and oxidative stress responses. Dysregulation of HAAO activity has been implicated in neurodegenerative disorders, inflammatory diseases, and cancer, highlighting its role in both physiological and pathological processes.
Recombinant HAAO protein is produced using genetic engineering techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells), enabling large-scale purification and functional studies. Its recombinant form retains enzymatic activity, allowing researchers to investigate substrate specificity, catalytic mechanisms, and interactions with inhibitors. This has facilitated drug discovery efforts targeting the kynurenine pathway, particularly for conditions like Alzheimer’s disease, HIV-associated neurocognitive disorders, and autoimmune diseases.
Structurally, HAAO belongs to the non-heme iron-dependent dioxygenase family, requiring Fe²⁺ as a cofactor for oxidative cleavage. Recent structural studies using X-ray crystallography or cryo-EM have revealed conformational details of its active site, guiding the design of selective modulators. Additionally, recombinant HAAO is utilized in diagnostic assays to measure enzyme activity in clinical samples, aiding biomarker research for inflammatory and neurological conditions.
Overall, HAAO recombinant protein serves as a vital tool for dissecting the kynurenine pathway's complexity and developing therapeutic strategies targeting its dysregulation in human diseases.
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