IntroductionThere are many antibodies in our body. However, we don't seem to talk about it too much. We just remember that it is a Y-shaped structure and can fight antigens. Therefore, we want to explore this topic further to find out how an antibody can be produced and how it can produce a large number of antibodies. In this study, we will review antibodies in different areas: the structure of the antibody, ways to affect antibody diversity, and the mechanisms of antibody generation and how to make them specific. Additionally, we have a future direction for the development of antibody technology to talk a little bit about this area. Antibody Structure As we all know, antibody is a type of protein with a Y-shaped structure. It consists of two heavy chains and one light chains (Roderick and Matthew, 2007). There are two types of light chains, one called Kappa and the other Lambda (Roderick, 2007). Heavy and light chains connect to each other using disulfide bonds. The function of the hinge region may allow antibodies to become more flexible. Heavy and light chains have a variable region and a constant region, the variable region can give the antigen binding specificity; while the constant region (also called isotype region) is determined by the mechanism of antigen destruction and guesses the infection time by setting the region of the constant region of antibodies. As noted in the USCSM (2010), hyper-variable region and framework region have a similar meaning to variable region and constant region. Germline and Somatic EventsHeavy chain and light chain arise from a set of genes that can be expressed both variable and constant. regions. The variable region contains three segments in the heavy chain which are V, D and J. V stands for variable, D s...... middle of paper ...... ts become very different from each other and can therefore further increase the diversity of antibodies.Future development and conclusionDue to the special function of antibodies, we want to make them to cure humans against antigens. However, at present, generating specific antibodies is a considerable waste of time and the cost is very high. Therefore, in the future, antibody products will be common and popular. In conclusion, the synthesis of antibodies is the same as that of proteins which is based on the central dogma: DNA produces mRNA then protein. Important points regarding the modification of functional activities of antibodies can be found in the DNA section. In these sections there are many methods for antibodies to become diverse and make them much more specific. In addition, future developments could make it possible to manufacture antibodies to treat the disease in a much more direct and safe way for humans...