paratopes
epitopes on the antigen while the paratopes on the antibody
An antibody (IgM for example is a pentamere), can consist out of more than one different immonoglobulines. One of the variabel regions of these immunoglobulines can bind to an epitope of an antigene, this is called affinity. When different variabel regions of one antibody bind to different epitopes on an antigene, the combined effect is called avidity. The effect is not equal to the sum of the affinity's.
An antibody can typically bind to two antigens at once.
it can be rised according to the epitopes present in antigen that enters our body..if separate antibody is rised to each specific epitope v call it as monoclonal antibody
An antibody can typically bind to one specific type of antigen.
part of an antigen moleculle inside our body. Example: antibody are bound because of epitopes.
An antibody may be unspecific to the protein it is produced against due to factors such as cross-reactivity, where its binding sites also recognize similar epitopes on different proteins. Additionally, if the antibody was generated in response to a complex antigen with multiple components, it might inadvertently bind to non-target proteins. Variations in the protein structure, such as post-translational modifications or misfolding, can also lead to unexpected interactions with the antibody.
When antibodies bind to the epitopes of an antigen(bacteria) via antigen receptors, the antibodies present the bacteria to a macrophages in a form that they recognize the foreign substance and engulf them. This antibody-antigen "team work" is also known as opsonization
Polyclonal antibody recognizes several epitopes on the target protein while monoclonal antibody recognizes only single epitope. Sometimes, monoclonal antibodies are not able to precipitate the antigen because the epitope might need to be exposed on the surface of the antigen to be recognized by the antibody. Since the epitope might be hidden and it's a single epitope that is recognized by the monoclonal antibody, the propability of the antibody to reconize the epitope is lower compared with the polyclonal antibody that recognizes several epitopes on the target protein.
Generally there are two antibodies used. Primary antibody which can bind specifically to the protein of interest. And a secondary antibody coupled with a detection system such as HRP that would bind the primary antibody and signals the presence of protein of interest.
It is the number of antigens one antibody molecule can bind to. For example, a trivalent antibody can simultaneously bind to three copies of the antigen it recognizes. This is not related to atomic valence.
Primary antibodies are specific in Western blotting because they are designed to bind to a particular target protein based on unique epitopes, or specific regions, on that protein. The specificity arises from the unique amino acid sequences and structural features of the target, which allow the primary antibody to recognize and bind with high affinity. This selective binding is crucial for accurately detecting and quantifying the target protein amidst a complex mixture of proteins, ensuring reliable results in analysis.