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Each antibody binds to a specific antigen in a highly specific interaction analogous to a lock and key.. An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as bacteria and viruses, including those that cause disease.
An antibody digested by papain yields three fragments, two Fab fragments and one Fc fragment An antibody digested by pepsin yields two fragments: a F(ab') 2 fragment and a pFc' fragment The fragment crystallizable region ( Fc region ) is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some ...
The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.
Humoral immunity is also referred to as antibody-mediated immunity. The study of the molecular and cellular components that form the immune system , including their function and interaction, is the central science of immunology .
Secondary antibodies provide signal detection and amplification along with extending the utility of an antibody through conjugation to proteins. [1] Secondary antibodies are especially efficient in immunolabeling. Secondary antibodies bind to primary antibodies, which are directly bound to the target antigen(s).
The "upper" part of an antibody. The complementarity-determining regions of the heavy chain are shown in red (Complementarity-determining regions (CDRs) are polypeptide segments of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively. CDRs are where these molecules bind to their ...
An antibody molecule. The two heavy chains are colored red, blue, and purple. The two light chains green and yellow. See also: The immunoglobulin light chain is the small polypeptide subunit of an antibody (immunoglobulin). A typical antibody is composed of two immunoglobulin (Ig) heavy chains and two Ig light chains.
The constant region is involved in effector function, while the variable region is involved in recognizing and binding to antigens. Anti-immunoglobulin antibodies may bind to either the variable or constant region of the immunoglobulin. [1] Anti-immunoglobulin antibodies are a type of secondary antibody.