Proteomics

Dataset Information

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Human chorionic villus proteome


ABSTRACT: We evaluated the effect of the different solubilization techniques on the reproducibility and width of the chorionic proteome characterized using bottom-up proteomics: SDS-based solubilization coupled with in-gel protein digestion after applying self-named 1DE gel-concentration procedure (SDS-PAGE without fractionating in the resolving gel for SDS removal) and in-solution protein digestion of urea-thiourea extracts. These results indicated that 1DE-concentration procedure coupled with in-gel digestion, LC-MS/MS and combinational usage of different bioinformatics tools provides in-depth analysis of a single protein band, including reliable identification and quantification of low-abundant proteins, e.g. FUCA1, PSG7.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Placenta

SUBMITTER: Olesya Larina  

LAB HEAD: Petushkova Natalia

PROVIDER: PXD024759 | Pride | 2022-06-17

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
070218PNA_03_180209151421_3_1_2.mgf Mgf
070218PNA_03_180209151421_3_1_2.raw Raw
070218PNA_03_180209164653_3_1_3.mgf Mgf
070218PNA_03_180209164653_3_1_3.raw Raw
070218PNA_03_3_1_1.mgf Mgf
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Publications

Protocol for Increasing the Sensitivity of MS-Based Protein Detection in Human Chorionic Villi.

Shkrigunov Timur T   Pogodin Pavel P   Zgoda Victor V   Larina Olesya O   Kisrieva Yulia Y   Klimenko Maria M   Latyshkevich Oleg O   Klimenko Peter P   Lisitsa Andrey A   Petushkova Natalia N  

Current issues in molecular biology 20220509 5


An important step in the proteomic analysis of missing proteins is the use of a wide range of tissues, optimal extraction, and the processing of protein material in order to ensure the highest sensitivity in downstream protein detection. This work describes a purification protocol for identifying low-abundance proteins in human chorionic villi using the proposed "1DE-gel concentration" method. This involves the removal of SDS in a short electrophoresis run in a stacking gel without protein separ  ...[more]

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