Antibody Fragment Booknotes (1) We conducted a mini literature review to learn more about fragment antigen binding (Fab) antibodies. Here’s what we found:Fab antibodies around 50 kDa in size are the antigen binding domains of an antibody molecule.Fab are the class of antibody fragments that have been most successful in clinical development and are the most thoroughly explored antibody fragment technology.Fab’ are fragments that contain disulfide bridge thiols, whereas fragments lacking the thiol functional group are called Fab.Fab fragments can be produced through two methods. The first is through enzymatic or chemical cleavage of the antibody. Secondly, they can be produced through the recombinant synthesis of F(ab’)2 antibody fragments followed by chemical reduction of these fragments.These fragments have applications in clinical toxicology, with potential to treat various toxins, such as digoxin. The selected fragments can completely bind digoxin in vivo.Recombinant Fab molecules are typically expressed in E. coli or yeast microbial systems.For Fabs containing the Fc region, Protein A can be successfully utilized for purification.For Fabs that do not contain an Fc region, mixed mode resins or cation exchangers can be used for capture.Protein L can be used for purification of antibody fragments, but is not as cost-friendly.
Antibody Fragment Booknotes (1) We conducted a mini literature review to learn more about fragment antigen binding (Fab) antibodies. Here’s what we found:Fab antibodies around 50 kDa in size are the antigen binding domains of an antibody molecule.Fab are the class of antibody fragments that have been most successful in clinical development and are the most thoroughly explored antibody fragment technology.Fab’ are fragments that contain disulfide bridge thiols, whereas fragments lacking the thiol functional group are called Fab.Fab fragments can be produced through two methods. The first is through enzymatic or chemical cleavage of the antibody. Secondly, they can be produced through the recombinant synthesis of F(ab’)2 antibody fragments followed by chemical reduction of these fragments.These fragments have applications in clinical toxicology, with potential to treat various toxins, such as digoxin. The selected fragments can completely bind digoxin in vivo.Recombinant Fab molecules are typically expressed in E. coli or yeast microbial systems.For Fabs containing the Fc region, Protein A can be successfully utilized for purification.For Fabs that do not contain an Fc region, mixed mode resins or cation exchangers can be used for capture.Protein L can be used for purification of antibody fragments, but is not as cost-friendly.
