Van Wyk J J, Bruton E T
Department of Pediatrics, University of North Carolina School of Medicine, Chapel Hill 27599, USA.
Endocrinology. 1997 Oct;138(10):4521-2. doi: 10.1210/endo.138.10.5578.
The anti-hIGF-I monoclonal antibody, alpha-sm1.2, was found to have substantial crossreactivity with human and rat IGF-II, but recognized rat IGF-I only when this ligand was present at very high concentration. (E50 for hIGF-I approximately 3.5 ng/tube vs. approximately 12,000 ng/tube for rat IGF-I). In the context of previous studies to define the epitope(s) of alpha-sm1.2, these findings point to the critical importance of aspartic acid at residue 20 in the B domain in determining the species and ligand specificity of this antibody. Previous studies using this antibody in rodent tissues may require reinterpretation in the light of these findings.
抗人胰岛素样生长因子-I（hIGF-I）单克隆抗体α-sm1.2被发现与人和大鼠的胰岛素样生长因子-II（IGF-II）具有显著的交叉反应性，但仅当大鼠IGF-I以非常高的浓度存在时才识别它。（hIGF-I的半数有效浓度（E50）约为3.5 ng/管，而大鼠IGF-I约为12,000 ng/管）。在先前确定α-sm1.2表位的研究背景下，这些发现表明B结构域中第20位残基的天冬氨酸在决定该抗体的物种和配体特异性方面至关重要。鉴于这些发现，先前在啮齿动物组织中使用该抗体的研究可能需要重新解释。
