title: Functional profiling of the proteome with affinity labels.
abstract: 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.
authors.affiliation: ActivX Biosciences, Inc., 11025 North Torrey Pines Road, La Jolla, CA 92037, USA. davidc@activx.com
authors.forename: David A
authors.initials: DA
authors.lastname: Campbell
authors.forename: Anna Katrin
authors.initials: AK
authors.lastname: Szardenings
mesh_terms: D000345:Affinity Labels; D000818:Animals; D003546:Cysteine Endopeptidases / Q000378:metabolism; D023281:Genomics / Q000379:methods*; D006801:Humans; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D020543:Proteome / Q000737:chemistry*; D012697:Serine Endopeptidases / Q000378:metabolism
chemical_list: D000345:Affinity Labels; D020543:Proteome; D010749:Phosphoprotein Phosphatases; D012697:Serine Endopeptidases; D003546:Cysteine Endopeptidases