Human Fc receptor panel - Biotin (ICH3019B)

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

ICH3019 is a Human Fc receptor panel: a collection of purified human Fc-receptor proteins supplied as a research reagent rather than a single antibody. Fc receptors are the cell-surface and soluble proteins that engage the fragment-crystallisable (Fc) region of immunoglobulins and translate antibody binding into biological effects. A panel format lets investigators compare, in parallel, how a given antibody or Fc-engineered molecule interacts across the family of receptors, which is central to understanding effector function, clearance and safety. Typical members of a human Fcgamma-receptor panel span the high- and low-affinity activating and inhibitory receptors and their common allelic variants, and neonatal FcRn is often included where recycling/half-life is of interest. Because it is a defined-protein reagent, the panel is intended for binding, screening and characterisation assays (for example ELISA, SPR/BLI, or cell-based readouts) rather than for administration to animals. This makes it well suited to biosimilar comparability, Fc-engineering and antibody developability workflows. Supplied research use only. Investigators should confirm the exact receptors, isoforms and allotypes included for their application. Fc receptors bind the Fc region of immunoglobulins and couple antibody recognition to downstream immune activity. The human Fcgamma receptor family comprises activating receptors that signal through immunoreceptor tyrosine-based activation motifs (for example the high-affinity FcgammaRI and the low-affinity FcgammaRIIa and FcgammaRIIIa) and the inhibitory FcgammaRIIb, which signals through an inhibitory motif; FcgammaRIIIb is GPI-anchored on neutrophils. The balance of activating versus inhibitory engagement governs effector functions such as antibody-dependent cellular cytotoxicity, phagocytosis and immune-complex clearance. Allelic variants (such as FcgammaRIIa H131/R131 and FcgammaRIIIa V158/F158) alter IgG-subclass affinity and can influence therapeutic-antibody activity. The neonatal receptor FcRn instead binds IgG in a pH-dependent manner to mediate recycling and prolong serum half-life. Together these receptors are key determinants of antibody potency, pharmacokinetics and biosimilar comparability.