Protein Detection
Protein Detection - Related Videos
09:00
Detection of Protein Ubiquitination
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Cited by 96 •
2009
Ubiquitination is a key posttranslational modification carried out by a set of three enzymes. Mutations of genes involved in this modification are associated with many different human diseases. Here, we describe protocols to detect protein ubiquitination in cultured cells in vivo and test tubes in vitro.
03:41
Fluorescence Anisotropy-Based Detection of Protein-Protein Interactions
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2025
In this video, we describe the fluorescence anisotropy technique to study the interactions between the fluorophore-tagged Shwachman-diamond syndrome (SBDS) protein and the elongation factor-like 1 GTPase (EFL1). On incubating SBDS proteins with gradually increasing concentrations of EFL1, a steady increase in anisotropy is observed, indicating a successful interaction between the two proteins.
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.
06:15
Biotinylated Cell-Penetrating Peptide Probe to Detect Protein-Protein Interactions
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2025
This video demonstrates a technique that uses biotinylated cell-penetrating peptides to detect intracellular protein-protein interactions. The cell-penetrating peptides facilitate the conjugated peptide to enter a cell and specifically bind to its interacting proteins. The biotin, after binding to avidin, allows purification of the interacting proteins’ complex from a cell lysate.
07:32
A Capillary Electrophoresis Immunoassay for Protein Biomarker Detection
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2025
This video demonstrates a capillary electrophoresis immunoassay protocol for detecting a protein biomarker associated with amyotrophic lateral sclerosis (ALS) from human blood platelets. Confirmation of the presence of the ALS biomarker protein is achieved through size-based separation of the platelet proteins followed by chemiluminescent detection.
FAQs
The key mechanistic step in many protein detection assays is selective binding between an antibody and its target protein. This interaction concentrates recognition on the protein of interest, while an attached or linked label produces a measurable readout. Because the signal is associated with target recognition, researchers can connect the observed measurement to protein presence in a complex biological sample.
Fluorescence and enzymatic color change provide distinct ways to convert molecular recognition into an observable signal. Fluorescent labels generate detectable light, whereas enzymatic labels produce a color change. In either case, signal intensity can support estimates of relative or absolute protein abundance, allowing researchers to select a readout suited to the measurement they need.
Protein detection can address several biological questions besides abundance. Fluorescence microscopy can show where a protein is located, while suitable analyses can examine protein expression, modification, or interactions. These dimensions help connect molecular measurements with cell structure and function, rather than treating a protein as an isolated quantity.
A typical workflow begins with a biological sample containing the proteins of interest. The method then applies a selective interaction or analytical measurement to identify the target, generates a detectable signal through fluorescence, enzymatic color change, or another label, and interprets signal intensity as an indication of abundance. The chosen platform determines which additional information can be obtained.
The choice depends on the biological question and the information required. Immunoassays support measurements based on selective binding, western blotting provides a protein-detection format, and fluorescence microscopy adds information about cellular localization. These approaches can therefore complement one another when researchers need to relate protein expression to spatial distribution or cellular processes.
Measurements of proteins can connect molecular changes with signaling pathways, biomarkers, pathogen biology, and responses to therapy. Researchers may use these results to examine how protein expression or modification changes during a biological condition or after treatment. Such findings help relate molecular observations to broader biological processes and potential clinical outcomes.