Dsred Epitope Ligand
Dsred Epitope Ligand - Related Videos
09:34
Intravital Imaging of Neutrophil Priming Using IL-1β Promoter-driven DsRed Reporter Mice
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Cited by 1 •
2016
This current protocol employs fluorescent reporters, in vivo labeling, and intravital imaging techniques to enable monitoring of the dynamic process of neutrophil priming in living animals.
13:58
Peptide:MHC Tetramer-based Enrichment of Epitope-specific T cells
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Cited by 28 •
2012
This protocol describes the use of peptide:MHC tetramers and magnetic microbeads to isolate low frequency populations of epitope-specific T cells and analyze them by flow cytometry. This method enables the direct study of endogenous T cell populations of interest from in vivo experimental systems.
02:40
Ligand Binding Sites
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2020
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands. Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
02:51
Metal-Ligand Bonds
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2020
The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes. In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
00:49
Ligand Binding and Linkage
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2020
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
FAQs
Selectivity comes from recognition of an exposed epitope within DsRed through specific, noncovalent interactions. Because the binding site is associated with the DsRed portion of a recombinant fusion, the ligand can capture that tagged protein even when other proteins are present. This molecular recognition provides enrichment beyond simply observing a fluorescent signal in the sample.
The ligand must be able to access the relevant DsRed epitope for binding to occur. An exposed epitope supports formation of the specific noncovalent interaction, whereas limited accessibility could reduce effective capture. This consideration matters when interpreting purification or detection results, because successful recognition depends on the target presenting the ligand-binding region in an accessible form.
Immobilization places the ligand on a solid support so that DsRed or a DsRed-tagged protein can be retained while unbound molecules are removed. The captured material can then be released by changing to defined elution conditions. This arrangement converts molecular recognition into a controllable capture-and-release process suitable for biochemical isolation.
A typical workflow begins by providing the ligand in an immobilized form, followed by contact with a sample containing DsRed or a DsRed-tagged protein. After binding, unbound molecules are removed, and the retained target is recovered through defined elution conditions. The sequence separates recognition, removal of nonbound material, and target collection.
Fluorescence can help track a DsRed-containing reporter or fusion, but it does not by itself provide biochemical enrichment or physical isolation. An epitope ligand adds selective capture, allowing the tagged protein to be concentrated from a complex sample and recovered for further analysis. It therefore complements fluorescence-based approaches when biochemical characterization is required.
The approach supports purification of recombinant DsRed-tagged proteins, selective detection of those proteins, and interaction studies in which associated behavior is examined after capture. By enriching the tagged target from a complex sample, ligand-based handling can make its presence and biochemical behavior easier to analyze than direct examination of the unfractionated material.