Article citationsMore>>

Zhao, Y., et al. (2009) Two routes for production and purification of Fab fragments in biopharmaceutical discovery research: Papain digestion of mAb and transient expression in mammalian cells. Protein Expression and Purification, 67, 182-189. doi:10.1016/j.pep.2009.04.012

has been cited by the following article:

• TITLE: Antibody fragments: Prolonging circulation half-life special issue-antibody research

  AUTHORS: Annabelle Patricia Herrington-Symes, Monika Farys, Hanieh Khalili, Steve Brocchini

  KEYWORDS: Antibody Fragment; Half-Life Extension; PEGylation; Fc Fusion

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.5, May 30, 2013

  ABSTRACT: Antibodies are currently the fastest growing class of therapeutic proteins. When antibody fragments are included, there are over thirty-five antibody-based medicines approved for human therapy. Many more antibody and antibody-like fragments are being evaluated clinically. Production of antibody fragments can be efficient and their compact size can allows for better tissue extravasation into solid tumors than full antibodies. Unfortunately, a key limitation of antibody fragments for systemic use is their short half-life in circulation. Prolonging their circulation half-life can be accomplished clinically by the covalent conjugation of the antibody fragment to the water-soluble polymer, poly(ethylene glycol) (PEG). Many polymers and strategies are also being pursued to increase antibody fragment half-life.