More About mAbs

What are mAbs?

  • Antibodies are unique proteins made by cells of the immune system to protect against repeated invasions by pathogenic microbes. Through their capacity to bind strongly to specific sites on microbes and mediate innate immune effector functions (complement, phagocytosis, ADCC), antibodies are able to specificities eliminate the invader. There are as many as 100 million antibodies with unique specificity within the human body. Each B cell is capable of making one type of antibody, meaning that 100 million B cell clones are needed to make all of the varieties of antibodies in the human body.

  • While the antibody producing B cells taken from the body are short lived, a number of techniques have been developed to immortalize the cells into antibody producing factories; the most common method is the production of hybridomas. Hybridomas can be grown in industrial size cell culture and the secreted monoclonal antibodies (mAbs) are easily purified from the culture media in almost unlimited quantities.

A Variety of Uses

Virtually all scientists use mAbs in their research today. They are used to identify the presence of proteins or for purification of the target protein. When linked with fluorescent tags, mAbs are used to analyze cell types in blood/tissue or for isolation of cells by flow cytometry. mAbs can be injected in mice to deplete specific cell types or block protein activity.

Almost all rapid diagnostic tests (influenza testing, pregnancy, rapid streptococcus test, etc.) are based upon mAbs binding. Antibodies used in these types of diagnostics are usually made using B cells from mice or rats. When mAbs began to be used in humans to block immune interactions, kill cancer cells, suppress transplant rejection or relieve autoimmune disease symptoms, it became clear that the mAbs made in species other than human would not be suitable as a result of an anti-species response. In order to be used effectively, methods were developed to humanize the mAbs.


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