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In immunology, the "immunoglobulin (a.k.a.

antibody) isotype" refers to the slight phenotypic variations within the immunoglobulin gene family that encode for variant immunoglobulin heavy chains and immunoglobulin light chains.

To be an isotype of a particular gene family means to belong to a set of genes that encode functionally similar proteins.

Usually, isotypes that belong to a particular gene family are duplicate copies of the same gene that arose because of a mistake during DNA replication.

As the species continues to evolve, those duplicated genes are passed on from generation to generation until every member of the species has a copy.

Each of those genes have since undergone mutations of their own, such that they diverge slightly in structure and function, giving rise to the different isotypes known today.

An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as bacteria and viruses.

The antibody recognizes a unique molecule of the harmful agent, called an antigen, via the Fab's variable region.

Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (similarly analogous to a key) on an antigen, allowing these two structures to bind together with precision.

Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by blocking a part of a microbe that is essential for its invasion and survival).

Depending on the antigen, the binding may impede the biological process causing the disease or may activate macrophages to destroy the foreign substance.

The ability of an antibody to communicate with the other components of the immune system is mediated via its Fc region (located at the base of the "Y"), which contains a conserved glycosylation site involved in these interactions.

The production of antibodies is the main function of the humoral immune system.

The enzyme-linked immunosorbent assay (ELISA) is a test that uses antibodies and color change to identify a substance.

Peptides (from Gr.: πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are biologically occurring short chains of amino acid monomers linked by peptide (amide) bonds.

Proteins (or) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.

Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another.

Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.