The National Cancer Institute seeks parties to license fully human antibodies for CH2-based research materials.
Recently, isolated immunoglobulin constant CH2 domains were proposed as scaffolds for construction of libraries containing diverse binders that could confer some effector functions. As a fragment in all IgGs, which are at high concentrations in blood, CH2-based therapeutics are likely to be well tolerated in therapeutic concentrations. CH2 binders can also be engineered to be selective so as to retain some of the effector functions that are possessed only by IgGs and not by other scaffolds.
NCI scientists discovered a novel fully human antibody (anti-CH2 Fab m01m1) that could be used safely in vitro and in vivo for the detection of CH2 and related targets, such as Fc and IgG. More specifically, anti-CH2 Fab m01m1 recognizes a conformational epitope on CH2 so it can be used to monitor conformational changes in CH2 and to select the proper folded isolated CH2 domains. Anti-CH2 Fab m01m1 is a powerful research reagent for developing CH2-based novel therapeutics (nanoantibodies, nAbs).