| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HMOX2 |
| Uniprot No | P30519 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-316aa |
| 氨基酸序列 | SAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE DGFPVHDGKG DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL AAGVALAAGL LAWYYM |
| 预测分子量 | 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HMOX2重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
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1. **标题**：*Cloning and Functional Characterization of Recombinant Human Heme Oxygenase-2 (HMOX2)*
**作者**：Smith A.B., et al.
**摘要**：本研究通过大肠杆菌系统成功表达并纯化重组人源HMOX2蛋白，证实其具有催化血红素分解为胆绿素和一氧化碳的活性，并揭示其酶动力学参数，为后续功能研究奠定基础。
2. **标题**：*Structural Insights into HMOX2 by X-ray Crystallography Using Recombinant Protein*
**作者**：Chen L., et al.
**摘要**：利用重组HMOX2蛋白进行X射线晶体结构解析，首次报道其三维构象，发现底物结合口袋的关键氨基酸残基，为靶向药物设计提供结构依据。
3. **标题**：*Tissue-Specific Expression of Recombinant HMOX2 in Mammalian Cell Lines*
**作者**：Yamamoto K., et al.
**摘要**：通过哺乳动物细胞表达系统制备重组HMOX2.发现其在大脑和睾丸组织中高表达，提示其在神经保护和生殖系统氧化应激调控中的潜在作用。
4. **标题**：*HMOX2 Recombinant Protein Attenuates Oxidative Damage in Cellular Models*
**作者**：Gomez-Ramos P., et al.
**摘要**：体外实验表明，外源性重组HMOX2蛋白可显著降低过氧化氢诱导的细胞氧化损伤，验证其在抗氧化治疗中的潜在应用价值。
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**注**：以上文献为示例性质，实际研究中请通过PubMed、Google Scholar等平台检索真实发表的论文。如需具体文献，建议提供更详细的研究方向或关键词。
Heme oxygenase 2 (HMOX2), a member of the heme oxygenase family, is a conserved enzyme critical for heme metabolism. It catalyzes the oxidative degradation of heme into biliverdin, carbon monoxide (CO), and free iron, with CO acting as a signaling molecule involved in vasodilation, anti-inflammation, and cytoprotection. Unlike the inducible isoform HMOX1. which responds to stressors like oxidative damage, HMOX2 is constitutively expressed across tissues, particularly in the brain, testes, and vascular endothelium, suggesting its role in maintaining cellular homeostasis under physiological conditions.
Recombinant HMOX2 proteins are engineered versions produced via heterologous expression systems (e.g., E. coli, mammalian cells) for research and therapeutic applications. These proteins retain enzymatic activity and structural integrity, enabling studies on heme degradation pathways, iron recycling, and CO-mediated signaling. Recombinant HMOX2 is pivotal in exploring its neuroprotective functions, as dysregulation has been linked to neurodegenerative disorders like Alzheimer’s and Parkinson’s diseases. Additionally, it serves as a tool to investigate oxidative stress responses, given its interplay with reactive oxygen species (ROS) scavenging mechanisms.
Recent studies highlight HMOX2's potential in mitigating ischemia-reperfusion injury and its regulatory effects on circadian rhythms via CO-dependent pathways. However, challenges persist in optimizing recombinant protein yield and stability for clinical translation. Advances in protein engineering and gene-editing technologies continue to refine HMOX2 production, aiming to harness its therapeutic potential in diseases involving heme toxicity or impaired antioxidant defenses. This enzyme remains a focal point in bridging basic biochemistry with biomedical innovation.
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