| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ELA2 |
| Uniprot No | P08246 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-267aa |
| 氨基酸序列 | IVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH |
| 分子量 | 52.6 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人ELA2蛋白的3篇示例参考文献，内容涵盖表达、功能研究及结构分析方向：
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1. **文献名称**：*High-yield production and characterization of recombinant human ELA2 in Pichia pastoris*
**作者**：Müller, T. et al.
**摘要**：研究通过毕赤酵母系统高效表达重组人ELA2蛋白，优化发酵条件实现可溶性表达，并验证其酶活性和稳定性，为工业化生产提供参考。
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2. **文献名称**：*Recombinant human neutrophil elastase exacerbates airway inflammation in murine asthma models*
**作者**：Chen, Y. & Wang, H.
**摘要**：利用重组hELA2蛋白处理小鼠模型，证明其通过激活IL-8和TNF-α通路加剧气道炎症，揭示了ELA2在哮喘中的潜在病理机制。
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3. **文献名称**：*Structural insights into the substrate specificity of recombinant human ELA2 through mutagenesis studies*
**作者**：Ito, S. et al.
**摘要**：通过点突变重组hELA2蛋白，结合分子动力学模拟，阐明其底物结合口袋的关键氨基酸残基，为设计高选择性抑制剂奠定基础。
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**注**：以上文献为示例性内容，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“recombinant human ELA2”或“recombinant neutrophil elastase”获取。
Recombinant human elastase 2 (rhELA2), also known as neutrophil elastase (NE), is a serine protease encoded by the ELANE gene located on chromosome 19. Naturally produced by neutrophils, ELA2 plays a critical role in innate immunity by degrading pathogens and remodeling extracellular matrix components, including elastin, collagen, and proteoglycans. Its enzymatic activity is tightly regulated to prevent tissue damage under normal conditions. Dysregulation of ELA2. however, is implicated in inflammatory diseases (e.g., chronic obstructive pulmonary disease, cystic fibrosis) and genetic disorders like cyclic and severe congenital neutropenia (SCN).
The recombinant form of ELA2 is engineered using expression systems like E. coli or mammalian cells, enabling large-scale production for research and therapeutic development. It retains catalytic properties similar to the native enzyme, making it essential for studying disease mechanisms, screening protease inhibitors, and modeling neutrophil-related pathologies. RhELA2 is also utilized in structural studies to understand its substrate specificity and interaction with endogenous inhibitors (e.g., α1-antitrypsin). Challenges remain in balancing its physiological roles with pathological effects, driving efforts to design selective modulators. As a research tool, rhELA2 advances both basic science and drug discovery, particularly in inflammation and neutrophil biology.
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