IgGand

IgGand is not a term recognized as a distinct molecule in mainstream immunology. As of 2024, no protein, gene, or approved therapy carries the exact name "IgGand." When this term appears in texts, it is usually a typographical error, a concatenation of "IgG" with another word, or a placeholder used in fictional or educational materials.

If the intention is to refer to immunoglobulin G (IgG), IgG is the major class of antibodies in human serum. It is composed of two heavy gamma chains and two light chains, with antigen-binding Fab regions and a Fc region that engages Fc receptors and complement. IgG antibodies mediate neutralization of pathogens, opsonization, and, for certain subclasses, activation of the classical complement pathway and antibody-dependent cellular cytotoxicity (ADCC).

There are four IgG subclasses in humans (IgG1–IgG4), differing in hinge region length and effector profiles. IgG antibodies are produced by plasma cells and have a half-life of about 21 days, largely because of recycling by the neonatal Fc receptor (FcRn). Clinically, IgG is the backbone of many monoclonal antibody therapies and is used in diagnostics and as a marker of immune response.

If "IgGand" appears in scientific writing, readers should check the surrounding context or references to determine whether the author intended "IgG" alone or a combination of IgG with another molecule (for example, "IgG and IgA" or an IgG-Fc fusion).

See also: Immunoglobulin G, Fc region, Fc gamma receptors, ADCC, Monoclonal antibodies, IgG subclasses.