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).
- Research reagent
- Facilitate the development of CH2-based novel therapeutics
- Can be used as a library for therapeutic candidates
- A novel fully human antibody for the detection of CH2
- CH2-based therapeutics are likely to be well tolerated in therapeutic concentrations
Dimiter Dimitrov Ph.D.
P. Prabakaran et al. Structure of an isolated unglycosylated antibody C(H)2 domain. [PMID 18931413]
D.S. Dimitrov, Engineered CH2 domains (nanoantibodies). [PMID 20046570]
R. Gong et al. Engineered human antibody constant domains with increased stability. [PMID 19307178]
X. Xiao et al. A large library based on a novel (CH2) scaffold: identification of HIV-1 inhibitors. [PMID 19615335]
G. Wozniak-Knopp et al. Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds. [PMID 22272277]
- Research Material: NIH will not pursue patent prosecution for this technology