Recombinant Human IgG2a protein

IgG2a is a subclass of immunoglobulin G (IgG) predominantly found in mice, playing a critical role in adaptive immune responses. As a key component of humoral immunity, it mediates pathogen neutralization, complement activation, and Fc receptor (FcγR)-dependent effector functions. Recombinant IgG2a proteins are engineered using genetic techniques to express specific antibody sequences in vitro, often in mammalian cell systems like CHO or HEK293 cells. This approach ensures precise control over antibody specificity, glycosylation patterns, and functional properties.

Structurally, recombinant IgG2a consists of two identical heavy chains (γ2a) and two light chains, forming a Y-shaped molecule. The variable regions of the heavy and light chains determine antigen-binding specificity, while the constant region (Fc domain) dictates interactions with immune cells. Compared to other IgG subclasses (e.g., IgG1 or IgG2b), murine IgG2a exhibits stronger binding to activating FcγRs (e.g., FcγRIV in mice) and enhanced complement-dependent cytotoxicity (CDC), making it particularly effective in clearing opsonized pathogens and tumor cells.

Recombinant IgG2a is widely used in biomedical research for developing therapeutic antibodies, studying immune mechanisms, and standardizing immunological assays. Its applications extend to cancer immunotherapy, infectious disease models, and autoimmune disorder studies. The recombinant format allows for site-specific modifications, such as Fc engineering to modulate antibody half-life or effector functions, and conjugation with fluorescent tags or enzymes for diagnostic purposes. Quality-controlled production ensures batch-to-batch consistency, addressing limitations of traditional hybridoma-derived antibodies. Ongoing advancements in protein engineering continue to expand its utility in both basic research and clinical development.