The first constant domain (CH1 and CL) of an antibody used as heterodimerization domain for bispecific miniantibodies

@article{Mller1998TheFC,
  title={The first constant domain (CH1 and CL) of an antibody used as heterodimerization domain for bispecific miniantibodies},
  author={Kristian M. M{\"u}ller and Katja M. Arndt and Wolfgang Strittmatter and Andreas Pl{\"u}ckthun},
  journal={FEBS Letters},
  year={1998},
  volume={422}
}

Fab Chains As an Efficient Heterodimerization Scaffold for the Production of Recombinant Bispecific and Trispecific Antibody Derivatives1

The use of the disulfide-stabilized L:Fd heterodimer as an efficient platform for production of intermediate-sized BsAbs and TsAbs in mammalian expression systems is proposed.

Improving the CH1-CK heterodimerization and pharmacokinetics of 4Dm2m, a novel potent CD4-antibody fusion protein against HIV-1

A combination of three approaches have successfully increased the persistence of 4Dm2m in mice and is the first report on stabilized CH1-CK, which is potentially useful as a new heterodimerization scaffold for generation of bispecific and multispecific proteins with a more favorable pharmacokinetic profile.

Development of a bispecific antibody tetramerized through hetero‐associating peptides

A novel method for constructing a highly functional antibody based on the hetero‐association of L27 domains that showed cytotoxic activity against EGFR‐expressing tumor cells by using CD16‐positive lymphocytes as effectors, and its cytotoxicity was comparable to that of a commercial therapeutic antibody.

Bispecific tandem diabody for tumor therapy with improved antigen binding and pharmacokinetics.

In vivo experiments indicated a higher stability and longer blood retention of tandem diabodies compared to single chain Fv fragments and diabody, properties that are particularly important for potential clinical applications.

Helix-stabilized Fv (hsFv) antibody fragments: substituting the constant domains of a Fab fragment for a heterodimeric coiled-coil domain.

The format of a helix-stabilized Fv (hsFv) fragment can be a useful alternative to existing recombinant antibody formats, especially in cases where poor expression of Fab fragments or multimerization of scFv fragments is a problem.

An efficient route to the production of an IgG-like bispecific antibody.

An efficient method is developed by using the natural dimerization mechanism between IgG heavy and light chains to produce a homogeneous bispecific IgG-like antibody product with each molecule containing four antigen binding sites, two for each of its target antigens.
...

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