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Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
ORGANISM(S): Homo sapiens (Human) 
2020-04-22 | PXD017030 | Pride
Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
ORGANISM(S): Bos taurus (Bovine) Oryctolagus cuniculus (Rabbit) Escherichia coli Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) Saccharomyces cerevisiae (Baker's yeast) Gallus gallus (Chicken) 
2020-04-22 | PXD017024 | Pride
Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
ORGANISM(S): Homo sapiens (Human) 
2020-04-22 | PXD017023 | Pride
Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
ORGANISM(S): Escherichia coli 
2020-04-22 | PXD017048 | Pride
Identification and characterization of Tryp-N, A thermostable protease for the production of N-terminal argininyl and lysinyl peptides
ORGANISM(S): Escherichia coli 
2020-04-22 | PXD017021 | Pride
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) 
To determine candidate OMA1 substrates during mitochondrial stress, OMA1 KO MEFs or its rescued cells expressing OMA1-Myc were treated with or without 40 uM FCCP for 2 h, then washed once with 1× PBS (pH 7.4), and cell pellets were collected. The pellets were then lysed in a guanidine buffer [6 M gu...
ORGANISM(S): Mus Musculus (mouse) 
Large-scale isolation of protein N-terminal peptides from LysargiNase digests was achieved by one-step strong cation exchange chromatography with disposable and parallel-processable pipette-tip columns. Novel cleavage sites for signal or transit peptides and non-canonical translation initiation site...
ORGANISM(S): Homo Sapiens (human) 
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