Sort   by:  
 Page size 
In this study, S-aminoethylation of Cys (AE-Cys) was carried out with 2-bromoethylamine to form pseudo-Lys, which was then digested with Lys-C or trypsin to improve proteome coverage in bottom-up proteomics. A model study with bovine serum albumin showed that the C-terminal side of Cys was successfu...
ORGANISM(S): Homo Sapiens (human) Bos Taurus 
Today, the most widely used bottom-up proteomics studies necessitate a proteolysis step prior to MS analysis. Trypsin is often the best protease in choice due to its high specificity and MS-favored proteolytic products. Trypsin has been challenged for its low cleavage efficiency at Lys-X bonds, and ...
ORGANISM(S): Homo sapiens (Human) 
2018-07-24 | PXD009797 | Pride
Bottom-up proteomics approach has become an important strategy in diverse areas of biological research, and the enzymatic digestion is essential for this technology. Endopeptidase Arg-C catalyzing the hydrolytic cleavage of peptide bonds C-terminal to arginine could be an important protease in botto...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2018-01-04 | PXD007994 | Pride
Urea-containing buffer solutions are generally used in proteomic studies to aid protein denaturation and solubilisation during cell and tissue lysis. It is well-known, however, that urea can lead to the carbamylation of peptides and proteins and; subsequently, incomplete digestion of proteins. In...
ORGANISM(S): Rattus rattus (Black rat) Homo sapiens (Human) 
2018-06-06 | PXD009426 | Pride
Zeins are a class of prolamine proteins extracted from maize, and are extensively used in the food and pharmaceutical industries. Therefore, characterization of its components is essential for quality control and safety evaluation. However, zein proteins have low abundance of the trypsin targets lys...
ORGANISM(S): Zea Mays 
2019-07-25 | PXD014743 |
Not available
2021-04-20 | MSV000076896 | MassIVE
SILAC-labeled immortalized mouse macrophages (IMMs) were LPS-stimulated. RNA-associated proteins were crosslinked to RNA using UV. RNA crosslinked proteins were purified, trypsin + Lys-C digested, and analyzed using LC-MS proteomics.
ORGANISM(S): Mus musculus (Mouse) 
2024-02-27 | PXD046754 | Pride
Background Plasma and cerebrospinal fluid CSF are complementary sources of biomarkers for neurodegenerative diseases. However, the wide dynamic range of protein abundances, particularly in plasma, hinders detection of low-abundance proteins. Depletion of high-abundance proteins and efficient enzymat...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2025-10-29 | MSV000099682 | MassIVE
this study employs two pairs of mirror ptoteases, trypsin/LysargiNase,and Lys-C/Lys-N to digest E.coli or yeast proteomes to evaluate a new software for de novo sequecing.
ORGANISM(S): Homo Sapiens Escherichia Coli Saccharomyces Cerevisiae 
2026-01-31 | PXD059331 |
Accurate characterization of the amino acid sequence and post-translational modifications (PTMs) of monoclonal antibodies (mAbs) is essential for evaluating product quality. Peptide mapping through bottom-up LC/MS analysis is a key methodology for this purpose. While trypsin is commonly the first ch...
ORGANISM(S): Homo Sapiens (human) 
Sort   by:  
 Page size