| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PAFAH1B2 |
| Uniprot No | P68402 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-229aa |
| 氨基酸序列 | SQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDTDGGFV HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA |
| 预测分子量 | 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. |
以下为假设性示例参考文献，供参考(建议通过学术数据库获取真实文献)：
1. **"Expression and Characterization of Recombinant PAFAH1B2 in E. coli"**
*作者：Zhang et al.*
*摘要：* 本研究成功构建了PAFAH1B2重组蛋白的原核表达系统，通过亲和层析纯化获得高纯度蛋白，并验证其酶学活性，为功能研究奠定基础。
2. **"Structural Insights into PAFAH1B2 by X-ray Crystallography"**
*作者：Smith et al.*
*摘要：* 利用重组PAFAH1B2蛋白解析了其晶体结构，揭示了底物结合位点的关键氨基酸残基，为靶向药物设计提供结构依据。
3. **"PAFAH1B2 Promotes Tumor Metastasis via Lipid Mediator Regulation"**
*作者：Lee et al.*
*摘要：* 通过体外实验证明，重组PAFAH1B2通过调控溶血磷脂酸(LPA)水平促进癌细胞迁移，提示其作为癌症治疗靶点的潜力。
4. **"Functional Screening of PAFAH1B2 Inhibitors Using Recombinant Protein"**
*作者：Chen et al.*
*摘要：* 基于重组PAFAH1B2建立高通量抑制剂筛选平台，发现多个小分子化合物可显著抑制其酶活性，具有抗炎治疗应用前景。
---
建议通过 **PubMed、Web of Science** 或 **Google Scholar** 检索实际文献，关键词：**PAFAH1B2 recombinant protein, expression, function**。
PAFAH1B2 (Platelet-Activating Factor Acetylhydrolase 1B2), also known as LIS1 homolog 2. is a member of the serine hydrolase superfamily. It shares structural homology with PAFAH1B1 (LIS1), a well-studied protein linked to neuronal migration disorders like lissencephaly. PAFAH1B2 is part of the intracellular PAFAH enzyme complex, which hydrolyzes platelet-activating factor (PAF), a potent lipid mediator involved in inflammation, immune responses, and cellular signaling. Unlike PAFAH1B1. which has established roles in brain development, PAFAH1B2’s biological functions remain less defined but are thought to overlap with and complement those of its homolog.
The recombinant form of PAFAH1B2 is typically produced using expression systems like *E. coli* or mammalian cells, enabling studies of its enzymatic activity, structure, and interactions. Recombinant PAFAH1B2 retains the catalytic triad (Ser-Asp-His) critical for its hydrolase activity, allowing researchers to investigate its substrate specificity and regulatory mechanisms. Emerging evidence suggests roles in cancer progression, neurodegeneration, and inflammation, with PAFAH1B2 overexpression observed in certain tumors, potentially influencing cell survival and drug resistance. Its interaction with microtubule-associated proteins also hints at involvement in cytoskeletal dynamics.
Research on recombinant PAFAH1B2 aids in deciphering its physiological and pathological relevance, offering insights into therapeutic targeting. However, functional redundancy within the PAFAH family and the lack of specific inhibitors pose challenges in delineating its unique contributions. Ongoing studies focus on structural characterization, post-translational modifications, and context-dependent roles in disease models, aiming to unravel its potential as a biomarker or therapeutic candidate.
×
