Jj. Vanwyk et Et. Bruton, MOLECULAR-BASIS FOR SPECIES AND LIGAND SPECIFICITY OF A MONOCLONAL-ANTIBODY RAISED AGAINST HUMAN IGF-I, Endocrinology, 138(10), 1997, pp. 4521-4523
The anti-hIGF-I monoclonal antibody, alpha-sm1.2, was found to have su
bstantial crossreactivity with human and rat IGF-II, but recognized ra
t IGF-I only when this ligand was present at very high concentration.
(E-50 for hIGF-I similar to 3.5 ng/tube vs. similar to 12,000 ng/tube
for rat IGF-I). In the context of previous studies to define the epito
pe(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 spec
ies and ligand specificity of this antibody. Previous studies using th
is antibody in rodent tissues may require reinterpretation in the ligh
t of these findings.