Proteomics

Dataset Information

0

Multiple experiments: Analysis of the HTPS FT; Kinetics of Thrombin and Chymotrypsin; Effect of temperature on Thrombin and Chymotrypsin


ABSTRACT: 1) Analysis of HTPS FT (analysis of the background, without protease) 2) Analysis of specificity and activity of Thrombin and Chymotrypsin at multiple time point (0,5,15,30,60,120,240 min) 3) Analysis of specificity and activity of Thrombin and Chymotrpysin with 2 hr incubation at 20C, 25C and 37C

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Federico Uliana  

LAB HEAD: Ruedi Aebersold

PROVIDER: PXD022972 | Pride | 2021-02-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
200908_QE1_mvizovisek_022.raw Raw
200908_QE1_mvizovisek_023.raw Raw
200908_QE1_mvizovisek_024.raw Raw
200908_QE1_mvizovisek_025.raw Raw
200908_QE1_mvizovisek_026.raw Raw
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Publications

Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen.

Uliana Federico F   Vizovišek Matej M   Acquasaliente Laura L   Ciuffa Rodolfo R   Fossati Andrea A   Frommelt Fabian F   Goetze Sandra S   Wollscheid Bernd B   Gstaiger Matthias M   De Filippis Vincenzo V   Auf dem Keller Ulrich U   Aebersold Ruedi R  

Nature communications 20210316 1


Proteases are among the largest protein families and critical regulators of biochemical processes like apoptosis and blood coagulation. Knowledge of proteases has been expanded by the development of proteomic approaches, however, technology for multiplexed screening of proteases within native environments is currently lacking behind. Here we introduce a simple method to profile protease activity based on isolation of protease products from native lysates using a 96FASP filter, their analysis in  ...[more]

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