| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PAF |
| Uniprot No | Q99487 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-392aa |
| 氨基酸序列 | MGVNQSVGFPPVTGPHLVGCGDVMEGQNLQGSFFRLFYPCQKAEETMEQPLWIPRYEYCTGLAEYLQFNKRCGGLLFNLAVGSCRLPVSWNGPFKTKDSGYPLIIFSHGLGAFRTLYSAFCMELASRGFVVAVPEHRDRSAATTYFCKQAPEENQPTNESLQEEWIPFRRVEEGEKEFHVRNPQVHQRVSECLRVLKILQEVTAGQTVFNILPGGLDLMTLKGNIDMSRVAVMGHSFGGATAILALAKETQFRCAVALDAWMFPLERDFYPKARGPVFFINTEKFQTMESVNLMKKICAQHEQSRIITVLGSVHRSQTDFAFVTGNLIGKFFSTETRGSLDPYEGQEVMVRAMLAFLQKHLDLKEDYNQWNNLIEGIGPSLTPGAPHHLSSL |
| 预测分子量 | 44 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3篇关于PAF(血小板活化因子)重组蛋白的参考文献摘要概括：
1. **"Cloning and expression of platelet-activating factor receptor"**
作者：Honda, Z., Nakamura, M., et al. (1991)
摘要：首次报道了PAF受体的分子克隆及重组表达，揭示了其跨膜结构和G蛋白偶联特性，为研究PAF信号通路奠定了基础。
2. **"Anti-inflammatory properties of recombinant platelet-activating factor acetylhydrolase (rPAF-AH) in sepsis"**
作者：Tjoelker, L.W., et al. (1995)
摘要：研究重组PAF乙酰水解酶在脓毒症模型中的抗炎作用，证明其通过降解PAF减轻全身炎症反应和器官损伤。
3. **"Recombinant PAF-acetylhydrolase attenuates acute pancreatitis in experimental models"**
作者：Lei, X., et al. (2005)
摘要：探讨重组PAF-AH对急性胰腺炎的治疗效果，发现其通过抑制PAF介导的炎症反应改善胰腺组织病理学和全身并发症。
注：以上为示例性概括，实际文献需通过PubMed或Web of Science检索确认具体信息。
**Background of PAF Recombinant Protein**
Platelet-activating factor (PAF), a potent phospholipid mediator, was first identified in the 1970s for its role in platelet aggregation and inflammatory responses. Structurally, PAF (1-alkyl-2-acetyl-sn-glycero-3-phosphocholine) consists of a glycerol backbone linked to an alkyl chain, an acetyl group, and a phosphocholine head. It exerts biological effects by binding to the PAF receptor (PAFR), a G protein-coupled receptor, triggering intracellular signaling pathways involved in immunity, inflammation, and cellular communication.
Recombinant PAF proteins are engineered using genetic or biochemical methods to mimic native PAF's structure and function. Advances in molecular biology, such as prokaryotic or eukaryotic expression systems, enable large-scale production of PAF or its analogs. These systems often involve inserting the PAF synthase gene or related sequences into host cells (e.g., *E. coli*, yeast, or mammalian cells), followed by purification via chromatography.
PAF recombinant proteins are critical tools for studying PAF's role in diseases like asthma, sepsis, atherosclerosis, and cancer. They facilitate receptor-binding assays, mechanistic studies, and drug screening. Additionally, recombinant PAF aids in developing therapeutic strategies, such as PAFR antagonists or anti-inflammatory agents. However, challenges remain in maintaining bioactivity due to PAF's instability and rapid metabolism *in vivo*.
Overall, PAF recombinant proteins bridge basic research and clinical applications, offering insights into lipid-mediated signaling and potential therapies for inflammation-related disorders. Their production and use underscore the intersection of biotechnology and pathophysiology in modern biomedical research.
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