Strong anion exchange fractionation

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Proteomics (73)
Unknown (11)
Other (2)
Transcriptomics (1)
Metabolomics (1)

Organisms

Aerococcus urinae NBRC 15544 = CCUG 36881 (48)
Andropogon gerardi (48)
Bacteria (48)
Bartonella quintana JK 31 (48)
Canis lupus familiaris (48)
Cnidaria (48)
Ectopseudomonas oleovorans CECT 5344 (48)
Ensifer adhaerens (48)
Halictus scabiosae (48)
Human immunodeficiency virus 1 (48)
Mesocricetus auratus (48)
Miscanthus x giganteus (48)
Morchella importuna (48)
Mus musculus (48)
Panicum virgatum (48)
Pseudomonas aeruginosa PA103 (48)
Pseudomonas aeruginosa SJTD-1 (48)
Rabies virus Nishigahara RCEH (48)
Rattus norvegicus (48)
Rattus rattus (48)
Rhodococcus jostii RHA1 (48)
Rhodopseudomonas palustris (48)
Shigella (48)
Sorghastrum nutans (48)
Streptococcus dysgalactiae subsp. equisimilis SK1249 (48)
Streptococcus pneumoniae (48)
Streptomyces coelicolor A3(2) (48)
Synechocystis sp. PCC 6803 (48)
Homo sapiens (24)
Saccharomyces cerevisiae (1)

Repository

pride (48)
PeptideAtlas (23)
GPMDB (2)
biostudies-arrayexpress (1)
jPOST (1)
MassIVE (1)
MetaboLights (1)

Tissue

Others (23)
Cell culture (11)
Epithelial cell (5)
Blood plasma (3)
Cell suspension culture (3)
Fibroblast (3)
Lung (3)
Whole body (3)
B cell (2)
Brain (2)
Breast cancer cell (2)
Endothelial cell (2)
Liver (2)
Astrocyte (1)
Blood platelet (1)
Breast epithelial cell (1)
Breast epithelium (1)
Cell line cell (1)
Cerebellar neuron (1)
Cholangiocyte (1)
Colon (1)
Embryonic stem cell (1)
Epithelial cell of prostate (1)
Flower (1)
Flower bud (1)
Follicular fluid (1)
HeLa cell (1)
Hepatocyte (1)
HiPSC cell (1)
Intestinal epithelium (1)

Disease

Breast cancer (6)
Disease free (3)
Not Available (2)
Lymphoma (2)
Alzheimer's disease (1)
Cholangiocarcinoma (1)
Influenza (1)
Onchocerciasis (1)
Pancreas adenocarcinoma (1)
Polycystic ovary syndrome (1)
Prostate adenocarcinoma (1)
Urinary bladder cancer (1)

Technology Type

Mass Spectrometry (48)
Shotgun proteomics (39)
SWATH MS (4)
Bottom-up proteomics (3)
Data-dependent acquisition (3)
Mass spectrometry (1)
Affinity purification coupled with mass spectrometry proteomics (1)
Data-independent acquisition (1)
Gel-based experiment (1)
MSE (1)
Top-down proteomics (1)

Instrument Platform

LTQ Orbitrap Elite (16)
QExactive (8)
Instrument (2)
Q Exactive (1)
Liquid Chromatography MS - negative (1)
Liquid Chromatography MS - positive (1)

Publication Date

2014 (24)
2018 (7)
2017 (6)
2015 (6)
2021 (5)
2023 (4)
2019 (4)
2016 (3)
2026 (3)
2025 (3)
2022 (3)
2020 (3)
2024 (2)
2013 (1)

UNIPROT ID/AC

A0A024RC46 (23)
A0A0C4DG89 (23)
A5A3E0 (23)
B3KML9 (23)
B3KT93 (23)
B4DHB3 (23)
B4DL86 (23)
B4DPR2 (23)
B4DRV9 (23)
B4E1R7 (23)
B4E3A4 (23)
D3DPU2 (23)
E5RK69 (23)
E7EX29 (23)
E9PAV3 (23)
G8JLB6 (23)
H0Y4R1 (23)
H0Y5C6 (23)
H0YAR2 (23)
H0YM50 (23)
H7BY16 (23)
H7BZ94 (23)
H7C144 (23)
I3L4N8 (23)
I3NI03 (23)
J3KPF3 (23)
J3KPS3 (23)
J3KRE2 (23)
J9JID7 (23)
O00148 (23)

ENSEMBL ID

ENSG00000170477 (19)
ENSG00000147251 (12)
ENSG00000247315 (8)
ENSG00000204131 (4)

CHEBI ID

CHEBI:86181, CHEBI:86137 (1)
CHEBI:86129, CHEBI:42027 (1)
CHEBI:85076, CHEBI:84234 (1)
CHEBI:83122 (1)
CHEBI:82724, CHEBI:83413 (1)
CHEBI:78268, CHEBI:79110 (1)
CHEBI:76325 (1)
CHEBI:76302, CHEBI:84746 (1)
CHEBI:75610, CHEBI:75577 (1)
CHEBI:74986, CHEBI:84839 (1)
CHEBI:74964 (1)
CHEBI:74910 (1)
CHEBI:74908 (1)
CHEBI:74907 (1)
CHEBI:74342, CHEBI:28610 (1)
CHEBI:73779, CHEBI:70744 (1)
CHEBI:73134, CHEBI:73004 (1)
CHEBI:73121, CHEBI:73008 (1)
CHEBI:68946, CHEBI:72651 (1)
CHEBI:65667 (1)
CHEBI:64554, CHEBI:27897 (1)
CHEBI:63961, CHEBI:57780, CHEBI:16462 (1)
CHEBI:60722 (1)
CHEBI:60286 (1)
CHEBI:60257, CHEBI:28229 (1)
CHEBI:60039, CHEBI:17203 (1)
CHEBI:58585, CHEBI:28718 (1)
CHEBI:58515, CHEBI:27592 (1)
CHEBI:58455, CHEBI:18347 (1)
CHEBI:58375, CHEBI:18095 (1)

Metabolite Name

Skatol (1)
Simvastatin lactone (1)
Phosphatidylcholine(18:0/18:1w9) (1)
GPCho(34:0) (1)
GPCho(18:3n3/18:3n3) (1)
GPCho(18:2w6/18:2w6) (1)
N-Stearoylethanolamide (1)
12-Hydroxy-Octadecanoic Acid (1)
L-Hexanoic acid ester with (3-carboxy-2-hydroxypropyl)trimethylammonium hydroxide inner salt (1)
(Z)-N-[(E,2S,3R)-1,3-bis(oxidanyl)octadec-4-en-2-yl]docos-13-enamide (1)
(3R)-3-[(Z)-octadec-9-enoyl]oxy-4-(trimethylazaniumyl)butanoate (1)
(-)-Tetradecanoylcarnitine (1)
L-gamma-glutamyl-l-alpha-aminobutyrylglycine (1)
N-(1,5-dimethyl-3-oxidanylidene-2-phenyl-pyrazol-4-yl)methanamide (1)
C18 Sphingomyelin (1)
OSF (1)
N-L-gamma-Glutamyl-L-tyrosine (1)
2-amino-5-[(1-carboxy-2-phenyl-ethyl)amino]-5-keto-valeric acid (1)
DAG(32:0) (1)
(2S)-3-(5-mercapto-3-methyl-imidazol-4-yl)-2-(methylammonio)propionate (1)
NODULARIN (1)
Phosphatidylserine(38:4) (1)
Phosphatidylserine(36:1) (1)
C16 sphingomyelin (1)
PE(18:0/20:4w6) (1)
Elthon (1)
(R)-Dodecanoylcarnitine (1)
22:0(2R-OH) (1)
26-oxidanylhexacosanoic acid (1)
1-Nitroso-Piperidine (1)

Modification

15.994915 (1)
57.021464 (1)

Study type

RNA-seq of coding RNA (1)

Release Date

2013 (3)
2021 (2)
2024 (1)
2023 (1)
2022 (1)
2017 (1)
2016 (1)
2014 (1)
2007 (1)

Lab affiliation

Max Planck Institute of Biochemistry (3)
CRUK Beatson Institute (2)
Division of Surgery, Oncology, and Pathology, Department of Clinical Sciences. Biomedical Center – Lund University, Solvegatan 19, 223 62, Lund, Sweden (2)
225, Veterinary Medical Center University of Minnesota 1365, Gortner Avenue St. Paul, MN 55108 (1)
Aalborg university (1)
Australian Proteome Analysis Facility, Macquarie University, NSW 2109, Australia (1)
Biochemical Proteomics Group, Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany (1)
Biological Mass Spectrometry Lab, Department of Translational Medicine (DiMeT), Center for Translational Research on Autoimmune & Allergic Diseases - CAAD, University of Piemonte Orientale - UPO (1)
Chair of Proteomics and Bioanalytics, Technical University of Munich (1)
College of Life Sciences, University of Dundee (1)
Department of Cell Biology Harvard Medical School Boston, MA 02115 (1)
Department of Cell Biology Harvard Medical School Boston, MA, USA (1)
Department of Clinical Science, Faculty of Medicine, University of Bergen, Norway (1)
Department of Infection Biology, Institute of Infection and Global Health, University of Liverpool. Liverpool, UK. (1)
Department of Infection Biology, Institute of Infection and Global Health, University of Liverpool, Liverpool, UK. (1)
Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI 48109, USA (1)
Department of Molecular Endocrinology, National Institute for Research in Reproductive Health, Indian Council of Medical Research, Mumbai 400012, India (1)
Department of Molecular and Cellular Hemostasis, Sanquin Research, Amsterdam, 1066CX, The Netherlands (1)
Department of Pharmacology and Chemical Biology Emory University School of Medicine Atlanta, GA, U.S. (1)
Department of Radiology Stanford University School of Medicine Canary Center at Stanford for Cancer Early Detection (1)
Department of System Biology, School of Life Sciences, Guangdong Provincial Key Laboratory of Cell Microenvironment and Disease Research, Shenzhen Key Laboratory of Cell Microenvironment, Southern University of Science and Technology, Shenzhen, 518055, China. (1)
Dept. Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, Munich, Germany (1)
EPFL Proteomics Core Facility (1)
Harvard Medical School Department of Cell Biology Harvard Medical School Boston, MA, USA (1)
Hubrecht Institute, KNAW (Royal Netherlands Academy of Arts and Sciences), Utrecht, The Netherlands (1)
Institute for Biochemistry and Molecular Biology, University of Bonn,Germany. (1)
Institute of Chemistry, Academia Sinica (1)
Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia (1)
Key Laboratory of Functional Protein Research of Guangdong Higher Education Institutes, Institute of Life and Health Engineering, College of Life Science and Technology, Jinan University (1)
Lab Head (1)

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Enhancing proteome coverage by using strong anion exchange in tandem with basic-pH reversed-phase chromatography for sample multiplexing-based proteomics

Sample multiplexing-based proteomic strategies rely on fractionation to improve proteome coverage. Tandem mass tag (TMT) experiments, for example, can currently accommodate up to 18 samples with proteins spanning several orders of magnitude, thus necessitating fractionation to achieve reasonable pro...

ORGANISM(S): Homo sapiens (Human)

2023-12-28 | PXD044393 | Pride

Label-Free Phosphoproteomics Profiling of Fission Yeast Schizosaccharomyces pombe

The phosphorylation of proteins modulates various functions of proteins and plays an important role in regulation of cell signaling. In the recent years, the label-free quantitative (LFQ) phos-phoproteomics has become the powerful tool to analyze the phosphorylation of proteins within the complex sa...

ORGANISM(S): Schizosaccharomyces pombe 927

2021-02-12 | PXD023818 | Pride

Pgc Schizosaccharomyces pombe Sax Lfq phosphoproteomics

Hydrophilic strong anion exchange (hSAX) chromatography for highly orthogonal peptide separation of complex proteomes.

Not available

S-EPMC3679572 | biostudies-literature

Label-Free Quantitative Phosphoproteomics of the Fission Yeast Schizosaccharomyces pombe Using Strong Anion Exchange- and Porous Graphitic Carbon-Based Fractionation Strategies.

Not available

S-EPMC7916215 | biostudies-literature

Trimodal chromatography enables facile peptide fractionation

We evaluated the utility of a trimodal stationary phase (Trinity P1) in offline peptide fractionation, and found it performed similarly to ion exchange or high pH reversed phase based techniques. It is orthogonal to low pH reversed phase and uses MS compatible mobile phase solvents.

ORGANISM(S): Homo sapiens (Human)

2017-08-07 | PXD006188 | Pride

Peptide fractionation Proteomics Trinity p1 Orthogonality 2d-lc Pancreatic cancer

Enhancing Proteome Coverage by Using Strong Anion-Exchange in Tandem with Basic-pH Reversed-Phase Chromatography for Sample Multiplexing-Based Proteomics.

Not available

S-EPMC11090996 | biostudies-literature

Proteomic profiling of over 13,000 proteins across ten mouse tissues using multi-dimensional peptide pre-fractionation

Proteome-wide abundance profiling across tissues can help to provide insight into the biological mechanisms underlying tissue-specific function and potential related dysfunction and amelioration thereof. Here, we use sample multiplexing to profile the proteomes of ten diverse mouse tissues using TMT...

ORGANISM(S): Mus musculus (Mouse)

2025-11-18 | PXD061609 | Pride

Tmtpro Tissue-specific expression Strong anion exchange fractionation Real-time search Peptide sax

Spin column-based peptide fractionation alternatives for streamlined tandem mass tag (SL-TMT) sample processing.

Not available

S-EPMC9990130 | biostudies-literature

Assembly of a marine viral metagenome after physical fractionation.

Not available

S-EPMC3620275 | biostudies-literature

Spin column-based prefractionation alternatives for Streamlined Tandem Mass Tag (SL-TMT) sample processing

Fractionation is essential to achieving deep proteome coverage for sample multiplexing experiments where currently up to 18 samples can be analyzed concurrently. However, prefractionation (i.e., upstream of LC-MS/MS analysis) with a liquid chromatography system constrains sample processing as only a...

ORGANISM(S): Homo sapiens (Human)

2023-12-28 | PXD038383 | Pride

Faims Tmtpro Hprp Isobaric tagging Sax

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88 Results

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