| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ELA2B |
| Uniprot No | P08218 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-269aa |
| 氨基酸序列 | MLGGEEARPNSWPWQVSLQYSSNGQWYHTCGGSLIANSWVLTAAHCISSSGIYRVMLGQHNLYVAESGSLAVSVSKIVVHKDWNSDQVSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGALPDDLKQGQLLVVDYATCSSSGWWGSTVKTNMICAGGDGVICTCNGDSGGPLNCQASDGRWEVHGIGSLTSVLGCNYYYKPSIFTRVSNYNDWINSVIANN |
| 预测分子量 | 28.4 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ELA2B(中性粒细胞弹性蛋白酶)重组蛋白的3篇参考文献示例：
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1. **标题**: *Expression and characterization of recombinant human neutrophil elastase in Escherichia coli*
**作者**: Li Y, et al.
**摘要**: 研究报道了利用大肠杆菌表达系统高效表达重组人中性粒细胞弹性蛋白酶(rhELA2B)，并通过亲和层析纯化获得高活性蛋白，验证了其酶活性和底物特异性。
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2. **标题**: *Structural insights into the catalytic mechanism of neutrophil elastase using a recombinant proform*
**作者**: Korkmaz B, et al.
**摘要**: 通过重组表达ELA2B酶原形式(pro-ELA2B)，解析其晶体结构，揭示了酶原激活过程中的构象变化及催化活性关键位点。
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3. **标题**: *Recombinant neutrophil elastase as a tool for studying inflammatory lung disease pathogenesis*
**作者**: Taggart CC, et al.
**摘要**: 利用重组ELA2B蛋白模拟肺部炎症环境，研究其与气道黏液蛋白的相互作用，探讨其在慢性阻塞性肺病(COPD)中的作用机制。
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注：以上文献为示例，实际引用时需核对真实出版物信息。建议通过PubMed或Web of Science以关键词“recombinant neutrophil elastase”或“ELA2B recombinant”检索最新研究。
**Background of ELA2B Recombinant Protein**
ELA2B, also known as Elastase 2B or neutrophil elastase (NE), is a serine protease primarily secreted by neutrophils. It plays a critical role in innate immunity by degrading microbial pathogens and modulating inflammatory responses. However, dysregulation of ELA2B activity is linked to tissue damage in conditions such as chronic obstructive pulmonary disease (COPD), cystic fibrosis, and acute lung injury.
Recombinant ELA2B protein is engineered *in vitro* using genetic cloning techniques to express and purify the enzyme for research and therapeutic applications. The gene encoding ELA2B is inserted into expression vectors, which are then transfected into host systems like *E. coli* or mammalian cell lines. Post-translationally modified forms, crucial for enzymatic activity, often require eukaryotic systems to ensure proper folding and glycosylation.
This recombinant protein is widely used to study ELA2B’s biological functions, including its interaction with substrates like elastin, collagen, and antimicrobial peptides. It also serves as a tool for screening inhibitors, aiding drug development for ELA2B-related diseases. Additionally, recombinant ELA2B assists in structural studies to map active sites or design targeted therapies.
A key advantage of recombinant ELA2B is its high purity and consistency compared to native proteins isolated from human tissues, reducing batch variability. It also circumvents ethical concerns associated with sourcing from biological fluids. Recent advancements in protein engineering have further optimized its stability and activity, enhancing its utility in both basic research and clinical applications.
In summary, recombinant ELA2B protein provides a reliable and scalable platform to explore the enzyme’s role in health and disease, offering potential pathways for therapeutic intervention in inflammatory and degenerative disorders.
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