constant region

Each antibody has a variable and a constant region.

The stem, the portion that gives it the Y-shape, is called the constant region.

Each heavy chain has two regions, the constant region and the variable region.

Heavy chains μ and ε have a constant region composed of four domains.

One possible solution is the use of antibody fragments containing just enough of the constant region to hold the molecule together.

The constant region is toward the base of the Y. The antibodies are proteins, built from amino acids.

The constant region is the handle of the key and is identical from one key to another of the same basic type.

Specific amplification was determined relative to constant region control PCR.

The Fc region is, therefore, sometimes incorrectly termed the "fragment constant region".

A researcher can generate several primary antibodies that recognize various antigens (have different variable regions), but all share the same constant region.

During class switching, the constant region of the immunoglobulin heavy chain changes but the variable regions, and therefore antigenic specificity, stay the same.

Different primary antibodies with different constant regions are typically generated by raising the antibody in different species.

Fcabs are molecules engineered from the constant region of an antibody (Fc) to contain an antigen-binding site.

It turns out that this constant region of the antibody that is primarily responsible for an allergic response when mouse antibodies are injected into humans.

Chimeric antibodies are composed of murine variable regions fused onto human constant regions.

This common attachment site provides a constant region of the flu virus for scientists to target in an effort to develop a so-called universal flu vaccine.

In immunology, the "immunoglobulin isotype" refers to the genetic variations or differences in the constant regions of the heavy and light chains.

The constant region is identical in all antibodies of the same isotype, but differs in antibodies of different isotypes.

This protein retains the specificity of the original immunoglobulin, despite removal of the constant regions and the introduction of the linker.

The Trap technology involves fusing two distinct fully human receptor components and a fully human immunoglobulin-G constant region.

If the constant region is replaced with the human form, the antibody is termed chimeric and the substem used is -xi-.

The domain was referred as "CεmX" to denote that it is part of the constant region of the membrane-bound ε chain of unknown function.

The remainder of the antibody structure is made up of constant regions, CL, CH, CH2 and CH3.

This mechanism relies on conserved nucleotide motifs, called switch (S) regions, found in DNA upstream of each constant region gene (except in the δ-chain).

The variable domain exon is rejoined through a process called non-homologous end joining (NHEJ) to the desired constant region (γ, α or ε).