Fragment crystallizable region
(Redirected from
Fc region
)The fragment crystallizable region (Fc region) is the tail region of an
polypeptide chain.[1][2] The Fc regions of IgGs bear a highly conserved N-glycosylation site.[3][4] Glycosylation of the Fc fragment is essential for Fc receptor-mediated activity.[5] The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2,6 linked sialic acid residues.[3]
The other part of an antibody, called the
Fab region
, contains variable sections that define the specific target that the antibody can bind. By contrast, the Fc region of all antibodies in a class are the same for each species; they are constant rather than variable. The Fc region is, therefore, sometimes incorrectly termed the "fragment constant region".
Fc binds to various cell
eosinophils; and other processes).[6]
Engineered Fc fragments
In a new development in the field of antibody-based therapeutics, the Fc region of
bispecific antibody (with both Fab and Fcab regions containing distinct binding sites). These bispecific monoclonal antibodies are sometimes referred to as mAb2.[8]
See also
- Antibody
- Fab region
- Protein tag
References
- ISBN 978-0-8153-3642-6.
- ISBN 978-0-8493-6078-7.
- ^ S2CID 22821543.
- S2CID 19147733.
- PMID 18566325.
- ISBN 978-1-4511-1783-7. Retrieved 31 December 2015.
- PMID 20150180.
- ^ "MAb2™ Bispecific Monoclonal Antibodies". Archived from the original on 2013-07-08. Retrieved 2013-08-13.