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The first epitope-based vaccine was developed in 1985 by Jacob et al. [28] Epitope-based vaccines stimulate humoral and cellular immune responses using isolated B-cell or T-cell epitopes. [28] [22] [17] These vaccines can use multiple epitopes to increase their efficacy. [28] To find epitopes to use for the vaccine, in silico mapping is often ...
The first use of epitope tagging was described by Munro and Pelham in 1984. [4] The FLAG-tag was the second example of a fully functional, improved epitope tag, published in the scientific literature. [1] [5] [6] and was the only epitope tag to be patented. [7] [8] It has since become one of the most commonly used protein tags in laboratories ...
Recognition of epitopes in a linear fashion. Note: the same (colored) segment of protein can be a part of more than one epitopes. In immunology, a linear epitope (also sequential epitope) is an epitope—a binding site on an antigen—that is recognized by antibodies by its linear sequence of amino acids (i.e. primary structure).
Each MHC molecule on the cell surface displays a small peptide (a molecular fraction of a protein) called an epitope. [3] The presented self-antigens prevent an organism's immune system from targeting its own cells. The presentation of pathogen-derived proteins results in the elimination of the infected cell by the immune system.
Note how the segments widely separated in the primary structure have come in contact in the three-dimensional tertiary structure forming part of the same epitope [1] In immunology, a conformational epitope is a sequence of sub-units (usually amino acids) composing an antigen that come in direct contact with a receptor of the immune system.
The HA-tag is a protein tag derived from the human influenza hemagglutinin (HA) protein, which allows the virus to target and enter host cells. An HA-tag is composed of a peptide derived from the HA-molecule corresponding to amino acids 98-106, which can be recognized and selectively bound by commercially available antibodies .
In immunology, epitope mapping is the process of experimentally identifying the binding site, or epitope, of an antibody on its target antigen (usually, on a protein). [ 1 ] [ 2 ] [ 3 ] Identification and characterization of antibody binding sites aid in the discovery and development of new therapeutics , vaccines , and diagnostics .
Therefore, proteins of dissimilar sequence may have a common structure which elicits an autoimmune response. It has been hypothesized that these virulent proteins display their mimicry through molecular surfaces that mimic host protein surfaces (protein fold or three-dimensional conformation), which have been obtained by convergent evolution.
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