Van Everbroeck B, O'Rourke K I, Cras P
Laboratory of Neurobiology, Born Bunge Foundation, University of Antwerp, Wilrijk, Belgium.
Eur J Histochem. 1999;43(4):335-8.
Monoclonal antibodies (Mab) to the prion protein (PrP) have been critical to the neuropathological characterisation of PrP-related diseases in human and animals. Although PrP is highly evolutionary conserved, there is some sequence divergence among species. We have analysed the F89/160.1.5 Mab raised against the bovine prion protein for immunoreactivity with the human prion protein. The antibody recognised the IHFG epitope of the prion protein. An analysis of the Swiss Prot database confirmed conservation of the epitope in humans. Further immunohistochemical (IHC) analysis showed a highly sensitive (final concentration 55 ng/ml) and specific antibody for prion detection in humans. The observed immunoreactivity of the prion protein did not differ from that observed after staining with the well-known 3F4 (Senetek) monoclonal antibody.
针对朊病毒蛋白（PrP）的单克隆抗体（Mab）对于人类和动物中与PrP相关疾病的神经病理学特征研究至关重要。尽管PrP在进化上高度保守，但不同物种之间仍存在一些序列差异。我们分析了针对牛朊病毒蛋白产生的F89/160.1.5单克隆抗体与人类朊病毒蛋白的免疫反应性。该抗体识别朊病毒蛋白的IHFG表位。对瑞士蛋白质数据库的分析证实了该表位在人类中的保守性。进一步的免疫组织化学（IHC）分析表明，该抗体对人类朊病毒检测具有高灵敏度（终浓度55 ng/ml）和特异性。观察到的朊病毒蛋白免疫反应性与用著名的3F4（Senetek）单克隆抗体染色后观察到的反应性没有差异。
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