Molecular basis for species and ligand specificity of a monoclonal antibody raised against human IGF-I

Endocrinology. 1997 Oct;138(10):4521-2. doi: 10.1210/endo.138.10.5578.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / analysis
  • Antibodies, Monoclonal / chemistry
  • Antibodies, Monoclonal / immunology*
  • Antibody Specificity*
  • Binding, Competitive
  • Cross Reactions
  • Epitopes / immunology
  • Humans
  • Insulin-Like Growth Factor I / analysis
  • Insulin-Like Growth Factor I / chemistry
  • Insulin-Like Growth Factor I / immunology*
  • Insulin-Like Growth Factor II / analysis
  • Insulin-Like Growth Factor II / chemistry
  • Insulin-Like Growth Factor II / immunology
  • Ligands
  • Mice
  • Molecular Sequence Data
  • Rats
  • Sheep
  • Species Specificity

Substances

  • Antibodies, Monoclonal
  • Epitopes
  • Ligands
  • Insulin-Like Growth Factor I
  • Insulin-Like Growth Factor II