Mouse immunoglobulin G2a (IgG2a) (IgG2a)

Mouse immunoglobulin G2a (IgG2a) is a subclass of murine immunoglobulin G (IgG) antibodies[1][2]. It is regarded as the "classical" or "canonical" IgG2 structure, characterized by four intact disulfide bonds in the hinge region[1]. IgG2a plays a key role in pathogen defense, primarily through opsonization (marking pathogens for phagocytosis), complement fixation (activating the complement cascade), and mediating immune effector functions[1]. It is one of the predominant isotypes produced in mice in response to infection with DNA or RNA viruses[6]. Structurally, IgG2a consists of two identical heavy chains (~50 kDa each) and two identical light chains (~25 kDa each), linked by disulfide bonds, forming a Y-shaped molecule with a total molecular weight of approximately 150,000 Da[1][5]. The Fc region of IgG2a can bind to the neonatal Fc receptor (FcRn), which helps prolong its half-life in circulation[2]. While IgG2a is not a therapeutic target itself, it is widely used as a research tool (e.g., isotype control, ELISA detection) and its levels are measured to study immune responses in various experimental models[3][4].

Other names

Immunoglobulin G2aIgG2a