C-myc Epitope
C-myc Epitope - Related Videos
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.
09:06
Isolation of the Side Population in Myc-induced T-cell Acute Lymphoblastic Leukemia in Zebrafish
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Cited by 5 •
2017
Here, we describe a technique to isolate the side population cells from a zebrafish model of myc-induced T-cell acute lymphoblastic leukemia (T-ALL). This side population assay is highly sensitive and is described for zebrafish T-ALL, but it may be applicable to other malignant and non-malignant zebrafish cell types.
08:09
Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
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Cited by 15 •
2017
Here, the authors present a simple and efficient protocol to define a linear antigenic epitope using a purified monoclonal antibody and peptide scanning through dot-blot hybridization. The identified epitope can then be used in therapeutic and diagnostic applications.
07:59
A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
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Cited by 21 •
2014
Biochemical assays with recombinant human MHC II molecules can provide rapid, quantitative insights into immunogenic epitope identification, deletion, or design. Here, a peptide-MHC II binding assay scaled to 384-well plates is described. This cost effective format should prove useful in the fields of protein deimmunization and vaccine design and development.
13:41
Use of Interferon-γ Enzyme-linked Immunospot Assay to Characterize Novel T-cell Epitopes of Human Papillomavirus
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Cited by 9 •
2012
Characterizing T-cell epitopes of pathogens that cause localized infections such as human papillomavirus is a challenge because of limited number of T cells in circulation. A method is described in which rare T cells were isolated and were characterized starting with a very small number of cells.
FAQs
The shared C-myc sequence provides a common antibody-recognition site on otherwise different recombinant proteins. When the antibody binds that sequence, the experimental signal identifies the tagged protein rather than relying on an antibody developed specifically against the protein's native structure. This standardizes detection across constructs and supports comparisons of expression or abundance.
A protein-specific antibody must recognize features of its individual target, whereas an anti-C-myc antibody can recognize the same inserted epitope on multiple recombinant proteins. This makes the tag useful when a suitable antibody against the protein of interest is unavailable. The approach shifts detection to the engineered tag while preserving selective identification of the recombinant product.
It acts as an identifier attached to the recombinant protein, allowing researchers to follow that protein through several analyses. Because the same tag can support detection, immunoprecipitation, immunofluorescence, and purification, results from expression, localization, interaction, and abundance studies can be connected to the same engineered protein.
In a Western blot, an antibody against the C-myc sequence provides the readout for a recombinant protein carrying the tag. Researchers can therefore confirm whether the construct is expressed and compare its apparent abundance across experimental conditions. The method is especially useful when direct detection of the recombinant protein with a protein-specific antibody is not available.
Immunofluorescence uses antibody recognition of the tag to visualize where the recombinant protein is located in cells. This connects the engineered protein to a cellular localization result without requiring an antibody against the protein itself. The approach helps researchers assess localization and compare distribution patterns among experimental samples or recombinant protein constructs.
Immunoprecipitation and protein purification extend tag-based analysis beyond simply observing a signal. Antibody recognition allows researchers to work selectively with the recombinant protein, while immunoprecipitation supports investigation of molecular interactions. These applications are valuable when experiments require examination of the tagged protein or its associated molecular context rather than only measuring expression.