Protocol for label-free quantitative lysine lactylproteome profiling
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Updated: May 16, 2025
Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
Published on: June 23, 2022
Yu Ran1, Qiqing Yang2, Lianqi Zhou2
1Department of Radiation Oncology and the State Key Laboratory of Transvascular Implantation Devices, the Second Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, China; The MOE Basic Research and Innovation Center for the Targeted Therapeutics of Solid Tumors, The First Affiliated Hospital, Jiangxi Medical College Nanchang University, Nanchang, China.
Abstract:
L-lactate has been recognized as an essential molecule for signaling and metabolic balance. Lactylation, a post-translational modification (PTM) derived from L-lactate, is commonly observed on various proteins and plays essential roles in cellular processes. Here, we present a protocol to globally profile the lactylation proteome and perform label-free quantification. We provide steps for cell preparation, protein extraction, digestion, peptide desalting, and lactylpeptide enrichment. Additionally, we outline the parameters for liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. For complete details on the use and execution of this protocol, please refer to Li et al.1.
