| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PAFAH1B3 |
| Uniprot No | Q15102 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-231aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSGEENP ASKPTPVQDV QGDGRWMSLH HRFVADSKDK EPEVVFIGDS LVQLMHQCEI WRELFSPLHA LNFGIGGDGT QHVLWRLENG ELEHIRPKIV VVWVGTNNHG HTAEQVTGGI KAIVQLVNER QPQARVVVLG LLPRGQHPNP LREKNRQVNE LVRAALAGHP RAHFLDADPG FVHSDGTISH HDMYDYLHLS RLGYTPVCRA LHSLLLRLLA QDQGQGAPLL EPAP |
| 预测分子量 | 28 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PAFAH1B3重组蛋白的3篇示例参考文献(注：文献信息为示例，建议通过学术数据库查询真实文献)：
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1. **文献名称**: *"Expression and functional characterization of recombinant PAFAH1B3 in inflammatory lipid metabolism"*
**作者**: Zhang L, et al.
**摘要**: 研究报道了PAFAH1B3重组蛋白在大肠杆菌中的高效表达与纯化，并证实其水解血小板活化因子(PAF)的酶活性，提示其在炎症相关脂质代谢中的潜在作用。
2. **文献名称**: *"PAFAH1B3 promotes cancer cell survival through PI3K/Akt signaling: Insights from recombinant protein-based assays"*
**作者**: Chen X, et al.
**摘要**: 通过重组PAFAH1B3蛋白的体外功能实验，揭示了该蛋白通过激活PI3K/Akt通路抑制肿瘤细胞凋亡，为癌症治疗提供了新靶点。
3. **文献名称**: *"Crystal structure of human PAFAH1B3 subunit and implications for inhibitor design"*
**作者**: Watanabe K, et al.
**摘要**: 利用重组PAFAH1B3蛋白解析了其三维晶体结构，阐明了酶活性位点的关键氨基酸残基，为开发特异性抑制剂奠定结构基础。
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**提示**：实际文献可通过PubMed、Web of Science等平台，以关键词“PAFAH1B3 recombinant”“PAFAH1B3 expression”或结合具体研究领域(如癌症、酶学)进行检索。
PAFAH1B3 (Platelet-Activating Factor Acetylhydrolase 1B3) is a subunit of the intracellular heterotrimeric PAFAH enzyme complex, which catalyzes the hydrolysis of platelet-activating factor (PAF) and related bioactive lipids. This serine hydrolase, also known as LIS4 or p30. is encoded by the PAFAH1B3 gene and plays a role in lipid signaling modulation. Unlike its neuronal homolog PAFAH1B1 (LIS1), which is critical for brain development, PAFAH1B3 is ubiquitously expressed and implicated in cancer progression, metabolic regulation, and inflammation. Recent studies highlight its overexpression in various tumors, including prostate, ovarian, and breast cancers, where it promotes tumor growth by altering lipid metabolism and enhancing cell survival pathways.
The recombinant PAFAH1B3 protein is engineered for in vitro studies to dissect its enzymatic activity, structural interactions, and pathological mechanisms. Produced via heterologous expression systems (e.g., E. coli or mammalian cells), it retains catalytic activity for substrate hydrolysis assays and inhibitor screening. Its recombinant form enables research into oncogenic lipid signaling, drug discovery for cancer therapeutics, and exploration of its non-catalytic roles in cellular processes. Additionally, PAFAH1B3's potential as a biomarker or therapeutic target in metabolic disorders is under investigation. The protein’s structure-function relationships, including its α/β hydrolase fold and catalytic triad, remain key focuses for biochemical characterization. Current efforts aim to develop selective inhibitors to probe its disease-associated functions, emphasizing its dual role in lipid homeostasis and pathological contexts.
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