Product Description

The Fc (fragment crystallizable) region is a structural domain composed of the constant regions of antibody heavy chains, playing central roles in immune effector functions. The Fc region functions by binding to Fcγ receptors (FcγR) or complement C1q, mediating antibody-dependent cell-mediated cytotoxicity (ADCC), complement-dependent cytotoxicity (CDC), and opsonophagocytosis. Glycosylation of the Fc region modulates its affinity and effector activity. Dysregulation of Fc-mediated functions is associated with autoimmune diseases and allergic reactions, whereas engineered Fc fragments (e.g., Fc fusion proteins) have been used to treat autoimmune diseases and cancers, underscoring the critical role of Fc in both immune defense and biotherapeutics.

Screeningbio’s TR-FRET Human Fc Detection Kit can be used for quantitative detection of human IgG or proteins with a human Fc tag in cell culture supernatants or after purification. This kit is a competitive immunoassay developed using TR-FRET technology, characterized by simplicity, rapidity, high accuracy, good reproducibility, and a wide detection range.

The basic principle of this method is as follows: a specific antibody against human Fc conjugated to TR-FRET Solar Eu*1 (donor) and human IgG conjugated to TR-FRET LA*2 (acceptor) are used. When the mAb anti‑hFc‑Solar Eu binds to Human IgG‑LA, the TR-FRET donor and acceptor are brought into close proximity, and upon excitation by an external light source, fluorescence resonance energy transfer occurs between them. Free human IgG or proteins with a human Fc tag in the sample can compete with Human IgG‑LA for the binding sites of mAb anti‑hFc‑Solar Eu. The signal intensity at a specific wavelength (665 nm) decreases with increasing concentrations of free human IgG or proteins with a human Fc tag in the sample.