Proteomics

Dataset Information

0

Mouse Cochlea Sensory Epithelium Proteome


ABSTRACT: The mouse cochlear sensory epithelium proteome has been characterized using FASP combined with GELFrEE and off-line SCX- and WAX-based methods follwed by nano LC-MS/MS. In addition, we utilzed single digestion and double digestion approaches using LysC and trypsin endoproteases. MS data files were processed with MaxQuant (Version 1.2.2.5, Max Planck Institute) and peak list files were searched by MASCOT search engine against the UniProt mouse database containing both forward and reversed protein sequences and common contaminants such as keratin. The initial parent and fragment ion maximum precursors were set to 6 ppm and 0.5 Da, respectively. The search included a fixed modification of carbamidomethyl of cysteine and variable modifications of oxidation of methionine and protein N-terminal acetylation. The minimum peptide length to be considered for identification was 6 amino acids.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Lancia Darville  

PROVIDER: PXD000231 | Pride | 2013-06-28

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
2012-09-19_AEX_Fraction01.RAW Raw
2012-09-19_AEX_Fraction02.RAW Raw
2012-09-19_AEX_Fraction03.RAW Raw
2012-09-19_AEX_Fraction04.RAW Raw
2012-09-19_AEX_Fraction05.RAW Raw
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Publications

In-depth proteomic analysis of mouse cochlear sensory epithelium by mass spectrometry.

Darville Lancia N F LN   Sokolowski Bernd H A BH  

Journal of proteome research 20130626 8


Proteomic analysis of sensory organs such as the cochlea is challenging due to its small size and difficulties with membrane protein isolation. Mass spectrometry in conjunction with separation methods can provide a more comprehensive proteome, because of the ability to enrich protein samples, detect hydrophobic proteins, and identify low abundant proteins by reducing the proteome dynamic range. GELFrEE as well as different separation and digestion techniques were combined with FASP and nanoLC-MS  ...[more]

Publication: 1/2

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