Use of ProteoMiner in Vetenery Research
Anna Marco Ramell, Gemma Rovira, Anna Maria Bassols Teixidó
Abstract
Anna Marco Ramell, Gemma Rovira, Anna Maria Bassols Teixidó
Abstract
sis of interacting partners of different proteins that are presented in TERMs [2]. This was accomplished by “pull-down” techniques and high-throughput protein trometry. For this end, synthetic biotinylated peptides spanning the C-terminal cytoplasmic end of these proteins were incubated with extracts from lymphoblast cell models, and then captured using Streptavidin-sepharose microbeads. Proteins interacting with the peptide baits were subjected to digestion and the resulting peptides systematically analyzed by HPLC-linear ion trap MS/MS mass spectrometry. Proteins from more
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sis of interacting partners of different proteins that are presented in TERMs [2]. This was accomplished by “pull-down” techniques and high-throughput protein trometry. For this end, synthetic biotinylated peptides spanning the C-terminal cytoplasmic end of these proteins were incubated with extracts from lymphoblast cell models, and then captured using Streptavidin-sepharose microbeads. Proteins interacting with the peptide baits were subjected to digestion and the resulting peptides systematically analyzed by HPLC-linear ion trap MS/MS mass spectrometry. Proteins from more
Key concepts: Biotinylation, Streptavidin, Chemistry, Mass spectrometry, Peptide, Sepharose, Chromatography, Cytoplasm