Anti-tmt Resin Enrichment
Anti-tmt Resin Enrichment - Related Videos
02:38
Anion Exchange Resin–Based Detection of Viruses from Bioaerosols
0 Views •
2026
Source: Schaeffer, J. W., Chandler, et al. Detection of Viruses from Bioaerosols Using Anion Exchange Resin. J. Vis. Exp. (2018).This video demonstrates the detection of viruses from bioaerosols using an anion exchange resin. A liquid impinger containing the resin is used to capture viruses from the air. The resin is collected and treated with a virus lysis buffer containing carrier RNA. The lysate is transferred to a microcentrifuge tube for viral RNA isolation, followed by qRT-PCR to amplify...
04:50
Phosphopeptide Enrichment: An Antibody-based Immunoprecipitation Technique to Separate Specific Phosphorylated Peptides from Complex Peptide Mixtures
0 Views •
2023
In this video, we demonstrate antibody-based immunoprecipitation of phosphopeptides from a peptide mixture. The enriched phosphopeptides are vacuum concentrated and stored for downstream analysis.
07:51
Acrylic Resin Molding Based Head Fixation Technique in Rodents
0 Views •
Cited by 4 •
2016
Traditional head fixation techniques have used metallic frames attached on the skull as an interface for head fixation apparatus. This protocol demonstrates a frameless, acrylic resin molding based head fixation technique for behavioral tasks in rodents.
13:58
Peptide:MHC Tetramer-based Enrichment of Epitope-specific T cells
0 Views •
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.
07:05
Clear Resin Casting of Arthropods for Use in Education, Outreach, and Research
0 Views •
2026
Here we show key steps in the process of creating high-quality, resin-embedded arthropods for educational instruction and outreach.
FAQs
TMT reagents covalently modify peptide N-termini and lysine residues, creating tag-bearing peptides that immobilized anti-TMT antibodies can recognize. Because the antibodies selectively bind this modification, labeled peptides can be separated from other components in a complex digest. This molecular recognition provides the basis for concentrating analytes before downstream mass-spectrometry analysis.
Selective capture reduces the number of unrelated molecules entering the analytical fraction, lowering sample complexity. At the same time, the process concentrates TMT-labeled peptides, which can make those analytes easier to detect during liquid chromatography-tandem mass spectrometry. The resulting enrichment is especially useful when the labeled peptides represent only part of a complex biological digest.
Immobilized anti-TMT antibodies retain peptides carrying the TMT modification, while unbound digest components remain available for removal during washing. Elution then releases the captured, enriched peptide fraction for analysis. These stages divide the workflow into selective retention, cleanup, and recovery, allowing the final sample to contain a greater proportion of TMT-labeled analytes.
TMT labeling supports comparison of protein abundance across multiple biological conditions, while resin enrichment concentrates the tagged peptide signals used for that comparison. By reducing sample complexity before mass spectrometry, the method can help researchers characterize labeled peptides and obtain quantitative protein measurements from multiplexed experiments. The enrichment therefore complements, rather than replaces, TMT-based quantification.
The workflow begins with a complex peptide digest whose N-termini and lysine residues have been covalently labeled with TMT reagents. The digest is then exposed to immobilized anti-TMT antibodies, followed by washing to remove unbound material. Researchers collect the enriched fraction after elution and subject it to liquid chromatography-tandem mass spectrometry.
The essential components are TMT-labeled peptides, an immobilized anti-TMT antibody resin, washing and elution steps, and a liquid chromatography-tandem mass spectrometry platform. The resin performs the affinity separation, whereas the analytical instrument examines the recovered peptide fraction. Together, these components connect selective biochemical enrichment with peptide detection and quantitative protein analysis.
Researchers can apply the method when they need to examine TMT-labeled peptides across different biological conditions and want a more focused analytical fraction. It is suited to multiplexed proteomics studies seeking peptide characterization and quantitative protein measurements. Enrichment is particularly relevant when reducing digest complexity and concentrating tagged analytes may support more informative mass-spectrometry results.