Surface Protein Profiling
Surface Protein Profiling - Related Videos
15:17
Colorectal Cancer Cell Surface Protein Profiling Using an Antibody Microarray and Fluorescence Multiplexing
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Cited by 19 •
2011
We described a procedure for the disaggregation of colorectal cancer (CRC) to produce viable single cells, which are then captured on customized antibody microarrays recognizing surface antigens (DotScan CRC microarray). Sub-populations of cells bound to the microarray can be profiled by fluorescence multiplexing using monoclonal antibodies tagged with fluorescent dyes.
08:07
Profiling of Surface Protein Epitopes on Viral Particles by Multiplex Dual-Reporter Strategy
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2024
Here, we describe a newly developed multiplex fluorescent immunoassay that uses a dual-reporter flow cytometric system to concurrently detect two unique spike protein epitopes on intact severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) viral particles that had been captured by angiotensin-converting enzyme-2-coupled magnetic microspheres.
09:35
Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
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Cited by 9 •
2017
Here we present protocols for affinity purification of protein complexes and their separation by blue native PAGE, followed by protein correlation profiling using label free quantitative mass spectrometry. This method is useful to resolve interactomes into distinct protein complexes.
10:02
Standardized SDS-PAGE Workflow for Personalized Protein Corona Profiling in Early Cancer Detection
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2025
This protocol standardizes SDS-PAGE analysis for personalized protein corona profiling on nanoparticles, enabling reproducible, scalable, and low-cost detection of cancer-specific signatures. Designed for early diagnosis of pancreatic ductal adenocarcinoma, it offers a practical, REASSURED-aligned alternative to complex proteomic methods in both research and clinical settings.
07:42
In-vivo Detection of Protein-protein Interactions on Micro-patterned Surfaces
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Cited by 7 •
2010
This video shows experiments with subsequent analysis of protein-protein interactions by the use of micro-patterned surfaces. The approach offers the possibility to detect protein interactions in living cells and combines high throughput capabilities with the possibility to extract quantitative information.
FAQs
Specificity comes from the interaction between a selected surface marker and its antibody or other affinity reagent. Once binding identifies the protein of interest, the resulting measurement can be quantified by flow cytometry, immunostaining, or a mass spectrometry-based approach. Using a set of markers rather than one measurement helps reveal patterns associated with cell identity, cellular state, and environmental interactions.
Surface protein profiling can distinguish related immune cell populations by comparing their marker patterns, while the same measurements can indicate activation or differentiation. This matters because a change in one protein may be less informative than a coordinated shift across several markers. In infection studies, those patterns also provide a way to examine how pathogens or inflammatory signals alter host cells.
The choice of readout affects how the profile is represented. Flow cytometry and immunostaining support affinity-reagent-based measurement of selected markers, whereas mass spectrometry-based approaches provide another route for profiling proteins. These methods serve as complementary options within the same investigative strategy, allowing researchers to identify and compare surface-protein patterns using different measurement platforms.
A basic workflow begins by choosing surface markers relevant to the cell population, infection, or inflammatory condition under study. Affinity reagents are then used to recognize those markers, followed by measurement with flow cytometry, immunostaining, or mass spectrometry-based analysis. Researchers compare the resulting profiles across samples to identify population differences or condition-associated changes.
In host-pathogen research, comparing surface-protein profiles can show how infection is associated with changes at the cell surface and can help characterize interactions between host cells and pathogens. The approach also supports examination of inflammatory effects by revealing marker patterns that differ between conditions. These comparisons connect cellular changes with broader immune responses during infection-related studies.
Recurring surface-marker patterns can support biomarker discovery by identifying features associated with particular disease states or immune-cell populations. The same comparisons can contribute to disease classification when profiles differ consistently between categories. In therapeutic research, proteins displayed on the cell surface may also be evaluated as potential targets, linking measurement of cellular features with treatment-oriented investigation.