Human monoclonal antibodies often display limited thermodynamic and colloidal stabilities.
This behavior hinders their production, and places limitations on the development of novel …

Many human monoclonal antibodies display poor biophysical properties, such as low
stability and a propensity to aggregate. These unfavorable tendencies can be even more …

Antibodies are highly soluble, multidomain proteins that are well suited for
biopharmaceutical development; however, engineering antibodies to perform novel …

The ability of antibodies to bind to target molecules with high affinity and specificity has led
to their widespread use in diagnostic and therapeutic applications. Nevertheless, a limitation …

Antibodies can have exquisite specificity of target recognition and thus generate highly
selective outcomes following their systemic administration. While antibodies can have high …

An antibody's stability greatly influences its performance (ie its specificity and affinity). Thus,
stability is a major issue for researchers and manufacturers, especially with the increasing …

Monoclonal antibodies are attractive therapeutics for treating a wide range of human
disorders due to their exquisite binding specificity and high binding affinity. However, a …

The widespread use of monoclonal antibodies for therapeutic applications has led to intense
interest in optimizing several of their natural properties (affinity, specificity, stability, solubility …

Antibody engineering to enhance thermostability may enable further application and ease of
use of antibodies across a number of different areas. A modified human IgG framework has …

The number of therapeutic monoclonal antibody in development has increased
tremendously over the last several years and this trend continues. At present there are more …