Fragment crystallizable region

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(Redirected from
Fc region
)
Fab fragments
and one Fc fragment
F(ab')2 fragment
and a pFc' fragment

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

References