纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | HO2 |
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. |
以下是模拟生成的3篇关于HO2(Heme Oxygenase-2)重组蛋白研究的参考文献示例,供参考格式和方向。实际文献需通过PubMed/Google Scholar检索获取:
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1. **标题**: "Expression and Purification of Recombinant Human Heme Oxygenase-2 in Escherichia coli"
**作者**: Smith J, et al.
**期刊**: *Protein Expression and Purification* (2010)
**摘要**: 本研究描述了一种在大肠杆菌中高效表达人源HO2重组蛋白的方法,优化了可溶性表达条件,并通过亲和层析纯化获得高纯度蛋白,为后续酶活研究奠定基础。
2. **标题**: "Structural Insights into Heme Oxygenase-2 Catalytic Mechanism by X-ray Crystallography"
**作者**: Chen L, et al.
**期刊**: *Journal of Biological Chemistry* (2015)
**摘要**: 通过X射线晶体学解析了HO2重组蛋白的3D结构,揭示了其血红素结合位点的关键氨基酸残基,并探讨了与HO1的结构差异对酶活调控的影响。
3. **标题**: "HO2 Recombinant Protein Attenuates Oxidative Stress in Neuronal Cell Models"
**作者**: Gupta R, et al.
**期刊**: *Free Radical Biology and Medicine* (2018)
**摘要**: 利用重组HO2蛋白处理神经元细胞,证明其通过降解血红素减少ROS生成,并激活Nrf2通路,提示HO2在神经退行性疾病中的潜在治疗价值。
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**建议**:实际研究中可通过以下关键词检索文献:
`"Heme Oxygenase-2 recombinant"`、`"HO2 protein expression"`、`"HO2 enzymatic activity"`。
数据库推荐:PubMed (https://pubmed.ncbi.nlm.nih.gov) 或 Web of Science。
HO2 recombinant protein is derived from heme oxygenase-2 (HO-2), a constitutive enzyme encoded by the HMOX2 gene. HO-2 is one of two isoforms (HO-1 and HO-2) responsible for catalyzing the rate-limiting step in heme degradation, converting heme into biliverdin, carbon monoxide (CO), and free iron. Unlike the inducible HO-1. which responds to cellular stress, HO-2 is ubiquitously expressed and plays a homeostatic role in regulating cellular heme levels, redox balance, and gasotransmitter signaling. Structurally, HO-2 contains heme-binding domains and unique cysteine residues that modulate its activity through post-translational modifications.
Recombinant HO-2 protein is typically produced using expression systems like E. coli or mammalian cells, enabling controlled studies of its enzymatic function and interactions. Researchers utilize this protein to investigate its role in physiological processes, including neuroprotection, vascular regulation, and anti-inflammatory responses mediated by CO and biliverdin-derived antioxidants. Its involvement in diseases such as Alzheimer's, hypertension, and metabolic disorders has spurred interest in therapeutic targeting. However, challenges remain in distinguishing HO-2-specific effects from HO-1 due to overlapping functions. Current studies focus on elucidating HO-2's signaling pathways, substrate specificity, and potential as a biomarker or drug target. Advances in recombinant technology continue to enhance the purity and functional characterization of HO-2. supporting both basic research and translational applications in oxidative stress-related pathologies.
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