All modules, mandatory or optional, could be downloaded from this section. More detail on these modules and installation information are accessible in Support section.
Proline server distribution contains Proline Server (the server Core module, Cortex), Proline Admin (for system administration purpose) and Sequence Repository (to gather proteins information from fasta files).
- Windows Full Installer: Installs Proline Server modules and optionally PostgreSQL server (for Windows OS). Require administration rights
- Windows Installer: Installs Proline Server modules (for Windows OS). PostgreSQL should already be installed, separately. No specific rights is require.
- Archive file: Contains archives for Proline Server modules. For manual installation or for Linux.
Proline Studio, the rich client interface, is distributed in a Zip file that must be extracted on each client computer.
Proline Web is the web client interface
Contains utilities to be used in complement of Proline Suite.
See documentation or forum message for more information.
The MS-Angel Graphical User Interface can be used to define data processing workflows involving several steps such as file conversions, MS/MS searches, search results import in Proline, Proline results validation & quantification.
Important note: it is mandatory to first install the Proline Web extension (see above) to take advantage of the MS Angel tool.
You can find the MS-Angel documentation here.
This tool allows user to easily convert raw files to mzdb (for XIC quantitation) and upload them on server side. This application embed the recommended version of raw2mzdb converter.
You can find the mzDB Wizard documentation here.
This application permits mzDB files visualization (chromatograms, scans, …). The corresponding documentation is available in the Proline User Guide (online here).
Samples (2 μg of yeast cell lysate + different spiked levels of UPS1) were analyzed in triplicate by nanoLC–MS/MS on an LTQ-Orbitrap Velos mass spectrometer. For more information on samples preparation and LC-MS/MS analyses, please refer to Ramus et al., J Proteomics. 2016 Jan 30;132:51-62. doi: 10.1016/j.jprot.2015.11.011.
|SAMPLE||RAW File||Mascot dat File||mzDB File|
|2µg levure UPS1 100fmol- Replicat 1||OEMMA121101_61b.raw||F083068.dat||OEMMA121101_61b.mzdb|
|2µg levure UPS1 100fmol- Replicat 2||OEMMA121101_63b.raw||F083069.dat||OEMMA121101_63b.mzdb|
|2µg levure UPS1 100fmol- Replicat 3||OEMMA121101_65b.raw||F083070.dat||OEMMA121101_65b.mzdb|
|2µg levure UPS1 10fmol – Replicat 1||OEMMA121101_36b.raw||F083064.dat||OEMMA121101_36b.mzdb|
|2µg levure UPS1 10fmol – Replicat 2||OEMMA121101_38b.raw||F083066.dat||OEMMA121101_38b.mzdb|
|2µg levure UPS1 10fmol – Replicat 3||OEMMA121101_40b.raw||F083067.dat||OEMMA121101_40b.mzdb|
Short protocol description:
Peaklist were generated using the Extract_msn.exe macro provided with Xcalibur. Peaklists were submitted to Mascot database searches (version 2.5.1). ESI-TRAP was chosen as the instrument, trypsin/P as the enzyme and 2 missed cleavages were allowed. Precursor and fragment mass error tolerances were set at 5 ppm and 0.8 Da, respectively. Peptide variable modifications allowed during the search were: acetyl (Protein N-ter), oxidation (M), whereas carbamidomethyl (C) was set as fixed modification. Databases used were yeast database from UniprotKB (S_cerevisiae_ 20121108.fasta, 7798 sequences), a compiled database containing the UPS1 human sequences (48 sequences) and the corresponding reversed databases in order to calculate FDR.