Dataset Information

Mouse_Hippocampus_LCMSMS_IEF_Pooling

ABSTRACT: Protein extract from a single mouse hippocampus was enzymatically digested and fractionated by isoelectric focusing. Aliquots of fractions were pooled to make fewer, more complex samples. The unfractionated lysate, fractions, and pooled fractions were subjected to liquid chromatography–mass spectrometry analysis. Samples consisting of many individual fractions had more protein identifications and quantified proteins with more spectral counts and greater precision than protein extract that was unfractionated or pooled into fewer LC-MS/MS samples.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain

SUBMITTER: Joseph Bundy

LAB HEAD: Richard Nowakowski

PROVIDER: PXD002905 | Pride | 2016-05-09

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	06282014_JLB_12F_A_Run1.raw	Raw
	06282014_JLB_12F_A_Run2.raw	Raw
	06282014_JLB_12F_A_Run3.raw	Raw
	06282014_JLB_12F_B_Run12.raw	Raw
	06282014_JLB_12F_B_Run2.raw	Raw

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Publications

Fractionation-dependent improvements in proteome resolution in the mouse hippocampus by IEF LC-MS/MS.

Bundy Joseph L JL Inouye Brian D BD Mercer Roger S RS Nowakowski Richard S RS

Electrophoresis 20160601 14

An assessment of fractionated mouse hippocampal peptides was conducted. Protein extract from a single mouse hippocampus was enzymatically digested and fractionated by IEF. Aliquots of fractions were pooled into fewer, more complex samples. The unfractionated lysate, fractions, and pooled fractions were subjected to LC-MS/MS analysis. Samples consisting of many individual fractions had more protein identifications, greater protein sequence coverage, and quantified proteins with more spectral coun ...[more]

PMID: 27129779

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