A label-free quantification experiment was performed to study the effect of R2PD1 chimeric protein treatment on the cellular proteome of Mel426 human melanoma cells. Peptides were separated by online reverse phase liquid chromatography and measured in an Exploris 480 Orbitrap mass spectrometer.
Mass spectrometry raw data were processed by MaxQuant software package (version 2.1.3.0) using its built-in Andromeda search engine. Mass spectra were searched against a target-decoy database consisting of the forward and reverse sequences of UniProt human reference proteome (release 2022_04; 102,601 entries) and a list of 246 common contaminants. Trypsin/P specificity was chosen. The minimum peptide length was set to be 7 amino acids. False discovery rate (FDR) was set to 1% for both peptide and protein identifications. MaxLFQ algorithm was employed for protein quantification.
[doi:10.25345/C5QJ78771]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: proteome, Mel426, melanoma, R2PD1
Principal Investigators: (in alphabetical order) |
Christof Niehrs, Institute of Molecular Biology, Germany |
Submitting User: | imbpcf |
Sun R, Meng Z, Lee H, Offringa R, Niehrs C.
ROTACs leverage signaling-incompetent R-spondin for targeted protein degradation.
Cell Chem Biol. Epub 2023 Jun 8.
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