**Background of PDE4B Recombinant Protein**
Phosphodiesterase 4B (PDE4B) is a member of the PDE4 enzyme family, which specifically hydrolyzes cyclic adenosine monophosphate (cAMP), a critical secondary messenger regulating cellular processes such as inflammation, immune response, and neuronal signaling. PDE4B plays a pivotal role in modulating cAMP levels, thereby influencing pathways linked to diseases like chronic obstructive pulmonary disease (COPD), asthma, depression, and schizophrenia. Its isoform-specific functions and tissue distribution make it a promising therapeutic target.
Recombinant PDE4B protein is engineered using heterologous expression systems (e.g., *E. coli*, insect, or mammalian cells*) to produce purified, functional enzyme for research and drug discovery. The protein typically retains key structural features, including catalytic domains responsible for cAMP hydrolysis and regulatory regions that influence substrate binding and inhibitor interactions.
Studies leveraging recombinant PDE4B aim to elucidate its structural biology, enzymatic kinetics, and interactions with inhibitors. For example, crystallographic analyses of recombinant PDE4B have revealed binding modes of selective inhibitors, guiding the design of therapeutics with reduced side effects compared to non-selective PDE4 blockers. Additionally, this protein is instrumental in high-throughput screening campaigns to identify novel modulators for inflammatory and neurological disorders.
The development of PDE4B recombinant protein also addresses challenges in isoform-specific targeting, as PDE4 subtypes (PDE4A, B, C, D) share high homology but differ in cellular roles. By enabling precise biochemical and pharmacological characterization, recombinant PDE4B advances the understanding of cAMP signaling dysregulation and fosters the development of targeted therapies, highlighting its importance in both basic research and translational medicine.
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以下是3篇关于Beta-amyloid 40(Aβ40)重组蛋白的相关文献摘要信息：
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1. **文献名称**：*"In vitro preparation of prefibrillar intermediates of amyloid-beta protein 40 and analysis of their toxicity"*
**作者**：Sambongi, K. et al.
**摘要**：描述了重组Aβ40蛋白的体外制备方法，通过调控pH和温度生成不同形态的预纤维中间体，并发现其可诱导神经元细胞氧化应激，毒性高于成熟纤维。
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2. **文献名称**：*"Structural characterization of beta-amyloid oligomer aggregates by NMR spectroscopy"*
**作者**：Chiti, F. & Dobson, C.M.
**摘要**：利用核磁共振(NMR)技术解析重组Aβ40寡聚体的动态结构，揭示其β-折叠构象的早期形成机制及其在阿尔茨海默病中的潜在致病作用。
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3. **文献名称**：*"Differences in β-amyloid 40 and 42 self-assembly revealed by hydrogen/deuterium exchange"*
**作者**：Bitan, G. et al.
**摘要**：比较重组Aβ40与Aβ42的聚集动力学，发现Aβ40倾向于形成可逆的低聚物，而Aβ42更易形成不可逆的纤维结构，解释了二者在神经毒性中的差异。
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这些研究聚焦于Aβ40的制备、结构及病理机制，为阿尔茨海默病研究提供了关键实验依据。
**Background of Beta-Amyloid 40 Recombinant Protein**
Beta-amyloid 40 (Aβ40) is a 40-amino acid peptide derived from the proteolytic cleavage of amyloid precursor protein (APP), a transmembrane glycoprotein. It is one of the major isoforms of beta-amyloid, alongside the more aggregation-prone Aβ42. Aβ40 is generated through sequential enzymatic processing of APP by β-secretase and γ-secretase. While Aβ40 is less hydrophobic than Aβ42. it remains a critical component in Alzheimer’s disease (AD) pathology, constituting the majority of soluble amyloid species in biological fluids.
Recombinant Aβ40 is widely used in research to study amyloid aggregation mechanisms, neurotoxicity, and therapeutic interventions. Its production typically involves heterologous expression systems, such as *Escherichia coli* or mammalian cells, followed by purification using chromatography techniques (e.g., HPLC or ion-exchange). Recombinant forms ensure consistency in experimental studies, avoiding variability inherent in synthetic peptides.
In AD, Aβ40 coexists with Aβ42 in amyloid plaques, though Aβ42 is more fibrillogenic and pathogenic. Aβ40’s role is dual: it may act as a "competitor" to mitigate Aβ42 aggregation, yet its overproduction or impaired clearance contributes to vascular amyloidosis (e.g., cerebral amyloid angiopathy). Studies also suggest Aβ40 has physiological functions, including synaptic regulation and antimicrobial activity, though these roles are less understood.
Research applications of recombinant Aβ40 include *in vitro* aggregation assays, cell culture models of toxicity, and *in vivo* studies using transgenic animals. It also serves as a reference in diagnostic assays to quantify Aβ levels in cerebrospinal fluid or blood. Despite its lower toxicity profile compared to Aβ42. Aβ40 remains a biomarker and therapeutic target due to its abundance and dynamic balance with Aβ42 in AD progression.
Overall, recombinant Aβ40 is a vital tool for unraveling amyloid biology and advancing AD therapeutics, bridging molecular insights with clinical translation.
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