epitope

Our criterion for an epitope was an average stimulation index of 3.0.

Each A domain can bind to a certain epitope of the target protein.

However, at any given time very few clones actually remain receptive to their specific epitope.

A small minority survives as memory cells that can recognize only the same epitope.

A cryptotope can also be referred to as a cryptic epitope.

An autoimmune response is then generated against the epitope.

Then this epitope can be effectively bound using an antibody on a filter paper.

Thus, a molecular feature on a virus antigen, an epitope, is a point in shape space.

We created a naturally occurring T cell epitope by comparison to a related protein.

It has been detected using its glycosylated epitope know as AC133.

Another similar method is followed, in which an epitope sequence is added to insert.

When the insert is expressed so is the epitope.

The part of an antibody that recognizes the epitope is called a paratope.

The two variable domains bind the epitope on their specific antigens.

About one antibody in a hundred thousand can bind a randomly chosen epitope.

Expression of an epitope on lipooligosaccharide is altered during growth as a biofilm.

Because of this property it causes an antibody response similar to the one elicited by the epitope.

Likewise, it is only paratope of the receptor that comes in contact with the epitope.

This motif is believed to be the T-cell epitope.

An antibody might bind that epitope and a family of similar shapes filling a ball in shape space.

Therefore, most antigens have the potential to be bound by several distinct antibodies, each of which is specific to a particular epitope.

The conformational epitope on hevein is called Hev b 6.02.

While this epitope exists within glycophorin C there it is a cryptanitgen.

In immunostaining methods, an antibody is used to detect a specific protein epitope.

In contrast, monoclonal antibodies are monovalent for the same epitope.