IntroductionThere are many antibodies in our body. However, we don't seem to exaggerate. Let's simply remember that it has a Y-shaped structure and can fight antigens. Therefore, we want to delve deeper into this topic to know how antibodies can be produced and how large numbers of antibodies can be produced. In this study we will look at antibodies in several areas: antibody structure, ways to influence antibody diversity, and mechanisms to generate antibodies and how to make them specific. Also, we have a future direction for the development of antibody technology to talk a little bit about this area. Structure of Antibodies As we all know, antibody is a type of protein with Y-shaped structure. It consists of two heavy chains and light chains (Roderick and Matthew, 2007). There are two types of light chains, one is called Kappa and the other is Lambda (Roderick, 2007). Both heavy and light chains connect to each other using disulfide bonds. The function of the hinge region may allow antibodies to become more flexible. Both the heavy and light chains have a variable region and a constant region, the variable region can provide specificity for antigen binding; while the constant region (also called isotype region) the mechanism to destroy the antigen and guess the infection time is determined by defining the region of the constant region of the antibodies. As stated on USCSM (2010), the hypervariable region and the framework region have a similar meaning as the variable region and the constant region. Germline and somatic events The heavy chain and light chain come from a set of genes that can be expressed in 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...... center of paper ...... become very different from each other so that it can increase further the diversity of antibodies.Future development and conclusionDue to the special function of antibodies, we want to produce them to treat humans against antigens. However, at this time generating specific antibodies takes a long time and the cost is very high. Therefore, antibody products will be common and popular in the future. To conclude, the synthesis of antibodies is the same as proteins which is based on the central dogma: DNA produces mRNA and then proteins. The important points of changing the functional activities of antibodies are found in the DNA section. In those sections there are many methods to allow antibodies to become different and make antibodies much more specific. Furthermore, future development can create antibodies that can treat the disease in a much more direct and non-harmful way for humans.