Human monoclonal antibody (mAbs) are emerging in the field of cancer therapy and have become an increasing proportion of new drugs that are recently approved. Although there are some methods to obtain antigen-specific mAbs from human B cells, it is generally impossible to directly immunize human beings with antigens of interest. For example, for infectious agents, those approaches are largely restricted. To solve these obstacles, two main approaches have been developed; either by humanizing antigen-specific antibodies from small experimental animals (which is laborious due to the great genetic differences from humans) or rely on the in vitro selection of antigen-specific binders from human antibody repertoires. However, the human mAbs developed by these methods are usually with low affinity.
We are now coming up with a much better idea that is humanizing non-human primates mAbs instead of murine mAbs. Due to the close genetic relationship with humans, immunized NHPs have more potential to be isolated with high affinity antibody to human target than other experimental species, such as mouse, rat and rabbit. In addition, with appropriate method, NHP antibodies are much<span> easier to be humanized</span> without any loss of affinity compared to widely used murine antibodies.
Resource: http://www.creative-biolabs.com/High-Affi-TM-Human-Antibody-Discovery.html
each of two or more forms of the same element that contain equal numbers of protons but different numbers of neutrons in their nuclei, and hence differ in relative atomic mass but not in chemical properties; in particular, a radioactive form of an element.
The allele combination for a female carrier is XRXr
Harmful, because there would not be enough resources