Dataset Information

Urea artifacts interfere with immunopurification of lysine acetylation

ABSTRACT: Urea-based buffers can induce carbamylation artefacts. Here we report that carbamylation of lysine residues resembles the structure of acetylated lysines (K-ac) and compete during K-ac immunoaffinity purification. We propose an alternative strategy using an ionic detergent which improves significantly the selectivity and efficiency of K-ac affinity immuno-purifications.

INSTRUMENT(S): Bruker Daltonics maXis series

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Ana Martinez

LAB HEAD: Javier Muñoz Peralta

PROVIDER: PXD003701 | Pride | 2017-01-11

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20151126_FG_AMVAcKCamKA1_1_2-B7_01_5628.d.zip	Other
	20151126_FG_AMVAcKCamKA2_1_2-B8_01_5638.d.zip	Other
	20151126_FG_AMVAcKCamKB1_1_2-B5_01_5627.d.zip	Other
	20151126_FG_AMVAcKCamKB2_1_2-B6_01_5637.d.zip	Other
	20151126_FG_AMVAcKCamKC1_1_2-B3_01_5625.d.zip	Other

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Urea Artifacts Interfere with Immuno-Purification of Lysine Acetylation.

Martinez-Val Ana A Garcia Fernando F Ximénez-Embún Pilar P Martínez Teresa-Calleja Ailyn A Ibarz Nuria N Ruppen Isabel I Munoz Javier J

Journal of proteome research 20170117 2

Comprehensive analysis of post-translational modifications (PTMs) often depends on the purification of modified peptides prior to LC-MS/MS. The implementation of these enrichment methods requires thorough knowledge of the experimental conditions to achieve optimal selectivity and sensitivity. In this regard, large-scale analysis of lysine acetylation, a key PTM for multiple cellular processes, makes use of monoclonal pan-antibodies designed against this moiety. We report that the immuno-purifica ...[more]

PMID: 28067524

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