Mucin Assay
Mucin Assay - Related Videos
11:39
Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution
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Cited by 39 •
2012
Unfixed frozen tissue samples embedded in Optimal Cutting Temperature medium (OCT) can be used to study natural distribution and glycosylation of secreted mucus. In this approach tissue processing is minimal and the natural presentation of glycolipids, mucins and glycan-epitopes is preserved. Tissue sections can be analyzed by immunohistochemistry using fluorescence or chromogenic detection.
09:24
Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins
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Cited by 32 •
2016
Mucins are high-molecular-weight glycoconjugates, with size ranging from 0.2 to 200 megadalton (MDa). As a result of their size, mucins do not penetrate conventional polyacrylamide gels and require larger pores for separation. We provide a detailed protocol for mucin agarose gel electrophoresis to assess relative quantification and study polymer assembly.
10:10
Robotic Duodenum-preserving Total Pancreatic Head Resection for Intraductal Papillary Mucinous Neoplasms
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2026
This protocol presents robotic duodenum-preserving total pancreatic head resection (R-DPPHRt) for intraductal papillary mucinous neoplasms (IPMNs). A video demonstrates the technique in a patient with main duct-IPMN, highlighting its feasibility as a minimally invasive, organ-preserving alternative to pancreaticoduodenectomy.
08:51
Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry
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2025
Here, we present a detailed protocol for the release of O-glycans from mucins, and the subsequent desalting, permethylation, and analysis using MALDI-TOF mass spectrometry.
08:12
The TUNEL Assay
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2023
One of the hallmarks of apoptosis is the nuclear DNA fragmentation by nucleases. These enzymes are activated by caspases, the family of proteins that execute the cell death program. TUNEL assay is a method that takes advantage of this feature to detect apoptotic cells. In this assay, an enzyme called terminal deoxynucleotidyl transferase catalyzes the addition of dUTP nucleotides to the free 3’ ends of fragmented DNA. By using dUTPs that are labeled with chemical tags that can produce...
FAQs
These formats detect different features of the target. Antibodies recognize mucin molecules, lectins bind carbohydrate structures associated with mucins, and chemical approaches estimate glycoprotein content. Consequently, results from different assay types may emphasize molecular identity, carbohydrate presentation, or overall glycoprotein abundance rather than represent interchangeable measurements in infection or barrier studies.
Mucin-associated carbohydrates provide binding targets for lectins and contribute to the glycoprotein signal measured by chemical detection. Changes in carbohydrate-related detection can therefore indicate altered mucin composition or glycosylation patterns, not simply a change in total mucin quantity. This distinction matters when evaluating epithelial responses to infection or inflammation.
The assay can reveal altered mucin levels associated with pathogen-induced secretion or mucin degradation, but the measurement must be interpreted in the biological context of the experiment. Comparing relevant biological samples and conditions helps relate the signal to epithelial production, release, or loss. This approach supports analysis of how pathogens affect mucosal defenses.
Mucins contribute to protective mucus barriers on epithelial surfaces and influence immune responses during infection. Measuring them alongside infection or inflammation-related conditions allows investigators to connect barrier changes with host-pathogen interactions. In immunology, this links epithelial defense measurements to broader questions about how mucosal tissues respond when exposed to pathogens.
Suitable biological materials include mucus, cell cultures, and tissue extracts. Mucus can reflect material present at an epithelial surface, whereas cell cultures support studies of epithelial secretion under controlled experimental conditions. Tissue extracts provide information from sampled tissue. Selecting among these sources should match whether the study focuses on barrier material, cellular responses, or tissue-associated changes.
Researchers can use these measurements to examine epithelial defense, pathogen-induced secretion, mucin degradation, and inflammation-linked changes in respiratory or intestinal disease models. The resulting data help characterize host-pathogen interactions and evaluate whether an intervention is associated with preserved or restored mucosal barrier function. Thus, the assay connects molecular measurements with disease-relevant barrier outcomes.