Monoclonal antibody

An antibody’s function in the immune system is to specifically bind foreign particles and to signal other cells to eliminate the foreign matter. An antibody’s ability to bind specifically is due to how strongly it can interact with the antigen. An antibody is able to bind with its antigen binding sites that are at the amino-terminal end of each branch of the molecule. The strength of the interaction between antibody and antigen is determined by the strength of interaction between the antibody and a single binding site and by the number of binding sites on the antigen. The strength of binding between the antibody(custom antibody servicehttp://www.ab-mart.com/absolution.html) and a single binding site is known as the antibody’s affinity for the antigen, and the binding is reversible. The affinity between the antibody and the antigen binding site is determined by the type of bond formed. Because an antigen can have multiple different epitopes, a number of antibodies can bind to the protein. When two or more antigen binding sites are identical, an antibody can form a stronger bond with the antigen than if only one of the antibody’s sites is bound. Antigens with multiple identical binding sites are called multivalent, and antibodies are able to bind it more strongly. This total binding strength is known as avidity, and is a measure of the strength of the interaction between the antibody and antigen.

The antigen binding portion of an antibody varies extensively among secreted antibodies, and this length of sequence is known as the variable region. The variable region construction during antibody production(custom monoclonal antibodieshttp://www.ab-mart.com/fast-custom-monoclonal-antibody_overview.html) in the B cell is what enables antibodies to be generated against an infinite variety of antigens. The other biological properties of the antibody and its role in signaling to other immune cells are determined by the constant regions of the heavy chains.