Recent studies have demonstrated the need for complementing cellular genomic information with specific information on expressed proteins, or proteomics, since the correlation between the two is poor. Typically, proteomic information is gathered by analyzing samples on two-dimensional gels with the s
Functional profiling of the proteome with affinity labels
โ Scribed by David A Campbell; Anna Katrin Szardenings
- Book ID
- 104414759
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 169 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1367-5931
No coin nor oath required. For personal study only.
โฆ Synopsis
The analysis of proteomic samples with affinity labels has been firmly established as a tool for the post-genomic researcher. Recent examples highlight the advantages of profiling functionally active members of specific protein families to identify therapeutically relevant protein targets that have escaped normal physiological regulation leading to increased or decreased activity. This dysregulation may result from any number of biological changes that modulate a protein's activity; for example, post-translational modifications of the protein or an imbalance between the protein and its endogenous inhibitor(s). By providing a direct measure of a protein's functional activity, affinity probe analysis identifies these changes and allows investigators to focus their research efforts upon those proteins that are most likely to be responsible for the biological changes under evaluation.
๐ SIMILAR VOLUMES
The combination of isotope coded affinity tag (ICAT) reagents and tandem mass spectrometry constitutes a new method for quantitative proteomics. It involves the site-specific, covalent labeling of proteins with isotopically normal or heavy ICAT reagents, proteolysis of the combined, labeled protein