- Capturem membrane technology
- Mass spectrometry digestion reagents
- His-tag purification
- Antibody purification
- Other tag purification
- Phosphoprotein and glycoprotein purification
- Expression systems
Mass spectrometry digestion with Capturem Trypsin and Pepsin
Mass spectrometry (MS) is the leading analytical technique used in proteomics for the characterization of proteins from a wide variety of organisms and cell types. The most critical step in MS analysis is sample preparation, which often requires the conversion of proteins to peptides. Rapid and complete digestion is important for detailed protein characterization. Trypsin is the most commonly used enzyme for proteolytic digestion of proteins to prepare peptides for analysis. It is a highly specific serine protease that cleaves at the carboxyl side of lysine and arginine residues, generating peptides of optimal size for MS analysis.
Mass spectrometry plays an important role in drug metabolism and pharmacokinetics (DMPK) studies, by allowing the identification and quantification of pharmaceutical compounds and their metabolites during the processes of absorption, distribution, metabolism, and excretion (ADME). Proteolytic digestion of therapeutic proteins using trypsin is a key step in preparing these proteins for MS analysis. Capturem Trypsin and Capturem Pepsin have been shown to provide much faster digestion than in-solution digestions with these enzymes, making them effective tools for high-throughput MS sample preparation that can increase the speed of DMPK studies and accelerate the process of drug discovery.
Fast, simple, and efficient protein digestion with Capturem Trypsin
Capturem Trypsin digests proteins more rapidly and completely than trypsin in solution, as demonstrated using apomyoglobin, a common protein mapping standard, and myoglobin, a tightly folded protein. This makes it a powerful tool for proteomic analysis. Apomyoglobin peptides generated by Capturem Trypsin digestion were shown to provide good sequence coverage using mass spectrometry, while digestion of a whole-cell lysate enabled the identification of 2,320 unique proteins via LC/MS-MS analysis.
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