Question is little bit confusing. Anyway I have an answer and hope it make sense to this question. Antibodies binds to a part of an antigen which is known as Epitope.
Antigen binding site or epitope is a part of an antigen that is recognized by the antibody. Paratope is a part of an antibody that binds on epitope.
No, not all antibodies can work with any antigen. Antibodies are highly specific in recognizing and binding to a particular antigen based on their unique binding sites. The binding of an antibody to an antigen is based on complementary shapes and charges, so a specific antibody will only bind to a specific antigen that matches its binding site.
Antigen binding is a region on an antibody that binds to antigens. Antigen binding is composed of one constant and one variable domain of each of the heavy and the light chain, and these domains shape the antigen binding site at the amino terminal end of the monomer.
The class of immunoglobulin to respond to the fist exposure of an antigen is immunoglobulin class M (IgM). While Immunoglobulin G (IgG) would predominate on the second exposure.
C stands for constant or conserved, V stands for variable. The variable part is what latches on to the antigen.
An adjuvant is a special binding substance that enhances immunogenicity and prolongs antigen retention at the injection site. It helps to stimulate a stronger immune response by promoting the activation of immune cells and improving the overall effectiveness of a vaccine.
Antibodies bind the antigen, which then targets the antigen for elimination by innate mechanisms
neutralization of the antigen, agglutination or precipitation, and complement activation.
Immunoglobulin genes undergo gene recombination and somatic hypermutation processes during B cell development. This leads to the generation of a diverse repertoire of antibodies with unique antigen-binding specificities. Additionally, the combination of different heavy and light chain gene segments contributes to the vast diversity of antibodies that can be produced.
Imunocompetent
Polyclonal antibody
Has no antigen in many textbooks it will state "no A-antigen and no B-antigen"(which imply the possibility of some other antigen) and some will even say, "no antigen" (which is true; antigens are things that attach to antigen binding sites, thus, if it does not fit any antigen binding sites, it is technically not a antigen but merely a "enzyme/protein") but this is just to reduce unnecessary and irrelevant information; they are only concerned about A-antibody, B-antibody, A-antigen, and B-antigen. Nonetheless, know that there are in fact antigens on o blood cells, they are just inactive. My guess is, N acetyl glactosamine on A antigen and Galactose on B antigens are Epitopes (: a small specific regions on antigens that are bound by the antigen receptors on lymphocytes and by secreted antibodies.) Antigens without epitopes will not be detected by antigen binding sites.