Antigen Unmasking
Antigen Unmasking - Related Videos
06:57
Development of an Antigen-driven Colitis Model to Study Presentation of Antigens by Antigen Presenting Cells to T Cells
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Cited by 9 •
2016
In this antigen-driven colitis model, OT-II CD4+ T cells expressing a red fluorescent protein were adoptively transferred into RAG-/- mice that express a green fluorescent protein in mononuclear phagocytes (MPs). The hosts were challenged with Escherichia coli (E.coli) expressing the ovalbumin protein (OVA) fused to a cyan fluorescent protein (CFP).
05:04
Viral Antigen Microarray Assay to Detect Antibody Isotypes in Serum Against Viral Antigen
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2025
In this video, we demonstrate the process for detecting antibody isotypes in multiple human serum samples using a microarray slide printed with antigenic subtypes of influenza virus strains.
08:09
Gene-environment Interaction Models to Unmask Susceptibility Mechanisms in Parkinson's Disease
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Cited by 10 •
2014
Lipoxygenase (LOX) isozymes can generate products that may increase or decrease neuroinflammation and neurodegeneration. A gene-environment interaction study could identify LOX isozyme-specific effects. Using the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) model of nigrostriatal damage in two LOX isozyme-deficient transgenic lines allows for comparison of the contribution of LOX isozymes on dopaminergic integrity and inflammation.
02:41
B Cell Activation on an Antigen-Coated Coverslip
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2025
This video demonstrates B cell activation in vitro. The process involves antigen interaction with B cell receptors, leading to cytoskeleton remodeling, immune synapse formation, lysosome movement, antigen internalization, processing, and subsequent presentation on MHC molecules for B cell activation.
08:32
Extraction of Tissue Antigens for Functional Assays
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2012
A simple protocol for preparing extracts of human tissue to be used as a source of antigens in functional T-cell assays is described. This method allows T-cell responses to tissue-derived antigens to be measured in vitro.
FAQs
Heat-induced treatment helps disrupt fixation-related crosslinks that can hide or alter antibody-recognizable epitopes. By restoring access to these regions, it can enable stronger antibody binding in tissue sections. The resulting signal may make target proteins easier to detect and localize, which supports more reliable interpretation in immunohistochemistry and immunofluorescence studies.
Proteolytic digestion uses enzymes to remove proteins that obstruct antibody access to epitopes altered or concealed during fixation. Unlike heat-induced treatment, this approach relies on controlled protein breakdown rather than heating. It provides an alternative route for exposing antibody-recognizable regions, allowing researchers to compare which preparation strategy produces more visible staining and clearer target localization in tissue sections.
Antibody binding depends on whether the recognizable epitope remains accessible after fixation. If fixation-related changes obscure that region, staining may be weaker and the target’s distribution harder to interpret. Restoring access can improve visualization of protein location within tissue, helping investigators interpret localization patterns and assess whether limited detectability reflects sample preparation rather than protein distribution.
It is applied during tissue sample preparation before antibody binding is evaluated. A section is exposed either to a heat-induced treatment or to proteolytic digestion, depending on the preparation strategy selected. After this step, improved epitope access can strengthen staining and support clearer detection and localization of proteins by immunohistochemistry or immunofluorescence.
Researchers can assess whether staining becomes stronger and whether the target protein’s location is easier to resolve in tissue sections. These outcomes are useful because immunohistochemistry and immunofluorescence depend on visible antibody-target interactions. Improved signal and localization can provide more interpretable evidence about protein distribution and the organization of biological structures within the prepared specimen.
By improving access to concealed or altered epitopes, the process supports detection of proteins in contexts where their distribution matters. In biology, this can aid studies of cell structure and disease mechanisms. In diagnostic research, stronger staining and clearer localization can assist investigations of biomarker expression in tissue specimens and improve interpretation of protein patterns.