Fc region

Fc region

[¦ef′sē ‚rē·jən]
(immunology)
Region of an antibody molecule that binds to antibody receptors on the surface of cells such as macrophages and mast cells, and to complement protein; Fcis derived from the term crystallizable fragment.
References in periodicals archive ?
This bispecific product candidate is a fully humanized IgG-scFv format antibody, licensed by Memorial Sloan Kettering to Y-mAbs, in which the anti-CD3 scFv is linked to naxitamab IgG1 and the Fc region is mutated to help prevent cytokine release as well as complement-mediated pain side effects.
Heavy-chain antisera probably target the Fc region, absent from idarucizumab.
One of the key components of bnAbs is the IgG Fc region. Using humanized mouse models, Halper-Stromberg et al.
Currently approved therapeutics also include an antibody Fab' fragment conjugated to a polyethylene glycol (PEG) (certolizumab pegol or Cimzia) [5-7] and a fifth biologic, etanercept or Enbrel, which comprises of a fusion protein of TNFRII and the Fc region of human IgG1 [8].
What is unique about this drug is that it is the only Fc-free, PEGylated anti-TNF Without this Fc region, it cannot be actively transported by the FcRn receptor on the placenta and, thus, results in minimal placental transmission.This suggests that certolizumab could be an option for treatment late in pregnancy without potential exposure to the newborn.
In this study we aimed to fuse the ctla-4 gene encoding the extracellular domain of CTLA-4 molecule with igg1 gene encoding Fc region of human IgG.
Cimzia is a small antibody, with a mass of about 40kDa (kilodaltons); therefore, it lacks the ability to cross-link, and it also lacks an Fc region. Clinical evidence suggests that Cimzia has an efficacy and safety profile similar to other TNF inhibitors, which may be attributable to its ability to penetrate inflamed joints more efficiently due to its small size.
Differences in glycosylation (generally present in the Fc region of the mAb) would be expected to impact mAb-Fc interaction with the FcyRIIIa.
As was shown in our studies of the past ten years, the proteins of human serum [epsilon]-globulin fraction exerted ability to chelate copper or zinc ions from the periglobular space and to pass because of such interactions through structural transformations with primary localization of them at the Fc region of the protein molecules [30, 31].
Fc region of IgY mediates most biological effector functions, such as complement fixation, anaphylactic reactions and opsonization, whereas the Fab region contains the antigen binding sites (DAVISON et al., 2008).