Human Antibody for Deploying CH2-Based Therapeutics

14:38 EDT 12 Jul 2018 | NIH

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).

NIH Ref. No.: 
  • A novel fully human antibody for the detection of CH2
  • CH2-based therapeutics are likely to be well tolerated in therapeutic concentrations
  • Research reagent
  • Facilitate the development of CH2-based novel therapeutics
  • Can be used as a library for therapeutic candidates
Development Status: 

Discovery (Lead Identification)

Updated On: 
Jun 7, 2018
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NCI - National Cancer Institute
DTDT Classification: 
Research Materials
DTDT Description: 
Research Materials
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PMID 18931413
PMID 20046570
PMID 19307178
PMID 19615335
PMID 22272277
Publication Title: 

P. Prabakaran et al. Structure of an isolated unglycosylated antibody C(H)2 domain. 

D.S. Dimitrov, Engineered CH2 domains (nanoantibodies). 

R. Gong et al. Engineered human antibody constant domains with increased stability. 

X. Xiao et al. A large library based on a novel (CH2) scaffold: identification of HIV-1 inhibitors. 

G. Wozniak-Knopp et al. Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds.

Collaboration Sought: 
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Licensing only

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Original Article: Human Antibody for Deploying CH2-Based Therapeutics


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