300 kda mwco - OmicsDI

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Proteomics (237)
Metabolomics (6)
Unknown (2)
Transcriptomics (1)

Organisms

Allexis (235)
Arabidopsis thaliana (235)
Homo sapiens (235)
Listeria monocytogenes (235)
Mus musculus (235)
Rattus norvegicus (235)
Saccharomyces cerevisiae (235)
Schizosaccharomyces pombe (235)
Shigella (235)
Shigella flexneri (235)
Staphylococcus aureus (235)
Aerococcus urinae NBRC 15544 = CCUG 36881 (234)
Alteromonadales (234)
Canis lupus familiaris (234)
Carya cathayensis (234)
Ensifer adhaerens (234)
Enterococcus faecalis (234)
Globicatella sanguinis (234)
Histomonas meleagridis (234)
Human immunodeficiency virus 1 (234)
Listeria monocytogenes EGD-e (234)
Methylohalobius crimeensis 10Ki (234)
Ophrys garganica (234)
Ophrys sphegodes (234)
Pseudomonas aeruginosa SJTD-1 (234)
Pseudomonas putida KT2440 (234)
Rhizobium sp. Leaf68 (234)
Schizosaccharomyces pombe 927 (234)
Cricetulus griseus (1)
Homo sapiens (1)

Repository

pride (235)
MetaboLights (6)
biostudies-arrayexpress (1)
jPOST (1)
MassIVE (1)

Tissue

Cell culture (39)
Blood serum (10)
Epithelial cell (9)
Brain (7)
Permanent cell line cell (7)
Blood plasma (6)
Leaf (6)
Photosynthetic cell (6)
Colon (5)
Liver (5)
Cell suspension culture (4)
Cerebrospinal fluid (4)
Hepatocyte (4)
Lung (4)
Root (4)
Urine (4)
Whole body (4)
Blood cell (3)
Bone marrow (3)
Gill (3)
Heart (3)
Plant cell (3)
Blood (2)
Embryonic stem cell (2)
Feces (2)
Fibroblast (2)
Flower (2)
HeLa cell (2)
Kidney (2)
Primary cell (2)

Disease

Breast cancer (3)
Disease free (3)
Hepatocellular carcinoma (3)
Alzheimer's disease (2)
Cardiovascular system disease (2)
Colon cancer (2)
Alopecia (1)
Amyotrophic lateral sclerosis type 1 (1)
Bladder disease (1)
Brain cancer (1)
Brain glioblastoma multiforme (1)
Cervical cancer (1)
Chronic myeloid leukemia (1)
Chronic obstructive pulmonary disease (1)
Dehydration (1)
Diphtheria (1)
FTDALS1 (1)
Influenza (1)
Lissencephaly 1 (1)
Lung adenocarcinoma (1)
Melanoma (1)
Obesity (1)
Ovarian cancer (1)
Pancreatic cancer (1)
Parasitic helminthiasis infectious disease (1)
Parkinson's disease (1)
Polycystic ovary syndrome (1)
Pre-eclampsia (1)
Prostate adenocarcinoma (1)
Prostate cancer (1)

Technology Type

Mass Spectrometry (235)
Shotgun proteomics (148)
Bottom-up proteomics (39)
Data-dependent acquisition (28)
Affinity purification coupled with mass spectrometry proteomics (17)
Data-independent acquisition (15)
Top-down proteomics (9)
Chemical cross-linking coupled with mass spectrometry proteomics (7)
Mass spectrometry (6)
Gel-based experiment (5)
SWATH MS (4)
SRM/MRM (3)
NMR spectroscopy (2)
MSE (2)
Metaproteomics (2)
DiaPASEF (1)
Glycoproteomics (1)

Instrument Platform

Liquid Chromatography MS - negative - reverse phase (2)
Liquid Chromatography MS - positive - reverse phase (2)
Illumina MiSeq (1)
QExactive (1)
Capillary electrophoresis MS – positive (1)
Tandem Gas Chromatography MS - positive (1)
Tandem Gas Chromatography MS - (1)
Flow injection analysis MS - positive (1)
Flow injection analysis MS - negative (1)
Nuclear Magnetic Resonance (NMR) (1)
Liquid Chromatography MS - (1)
Nuclear Magnetic Resonance (NMR) - (1)
Capillary electrophoresis MS - negative (1)

Publication Date

2023 (37)
2024 (34)
2022 (33)
2025 (30)
2026 (26)
2020 (19)
2021 (18)
2018 (16)
2019 (15)
2017 (7)
2016 (7)
2015 (2)

CHEBI ID

CHEBI:15428 (3)
CHEBI:15940 (3)
CHEBI:33508 (3)
CHEBI:28300 (3)
CHEBI:15741 (3)
CHEBI:25094 (3)
CHEBI:26271 (3)
CHEBI:16708 (3)
CHEBI:20067 (3)
CHEBI:76341 (2)
CHEBI:18300 (2)
CHEBI:22652 (2)
CHEBI:16016 (2)
CHEBI:15344 (2)
CHEBI:15603 (2)
CHEBI:17172 (2)
CHEBI:17748 (2)
CHEBI:17230 (2)
CHEBI:27266 (2)
CHEBI:15725 (2)
CHEBI:16199 (2)
CHEBI:422 (2)
CHEBI:15318 (2)
CHEBI:17780 (2)
CHEBI:18127 (2)
CHEBI:17561 (2)
CHEBI:17497 (2)
CHEBI:15971 (2)
CHEBI:16977 (2)
CHEBI:17148 (2)

Metabolite Name

Ornithine (2)
L-Leucine (2)
Nicotinamide (2)
Lysine (2)
L-Cysteine (2)
L-Methionine (2)
L-Histidine (2)
L-Alanine (2)
Putrescine (2)
D-Glucose (2)
L-Asparagine (2)
Glycine (2)
L-Threonine (2)
L-Tryptophan (2)
L-Serine (2)
Phosphoenolpyruvic acid (2)
Adenosine monophosphate (2)
L-Phenylalanine (2)
L-Tyrosine (2)
L-Glutamine (2)
L-Arginine (2)
Betaine (2)
Carnitine (2)
Guanine (2)
Creatine (2)
Choline (2)
L-Lysine (2)
L-Isoleucine (2)
L-Proline (2)
L-Valine (2)

Modification

-17.026549 (1)
15.994915 (1)
57.021464 (1)
79.966331 (1)

Study type

High-throughput sequencing (1)

Release Date

2021 (1)
2025 (1)
2024 (1)

Lab affiliation

North Carolina State University (16)
Proteomics Core Facility and Research Group Proteomics, CEITEC-MU, Masaryk University, Brno, Czech Republic (6)
1VIB-UGent Center for Medical Biotechnology, VIB, 9052 Ghent, Belgium 2Department of Biomolecular Medicine, Ghent University, 9052 Ghent, Belgium (4)
CEITEC-MU, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic (2)
Department for Plant Cell and Molecular Biology, Institute for Biology, Humboldt-Universität zu Berlin (2)
Department of Geoscience, University of Calgary, Calgary, AB, Canada; Department of Plant and Microbial Biology, North Carolina State University, Raleigh, North Carolina, USA (2)
Department of Molecular and Applied Microbiology Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute Jena, Germany (2)
Georgetown University Medical Center (2)
Institute of Biological Chemistry, Academia Sinica, Taipei, 115201, Taiwan Institute of Biochemical Sciences, National Taiwan University, Taipei, 106319, Taiwan International Institute for Sustainability with Knotted Chiral Meta Matter (SKCM2), Hiroshima University, Hiroshima, 739-8511, Japan (2)
Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology / Hans Knöll Institute Jena (Leibniz-HKI), Jena, Germany (2)
Plateforme protéomique 3P5-Necker, Université Paris Descartes - Structure Fédérative de Recherche Necker, INSERM US24/CNRS UMS3633, Paris 75014, France (2)
Proteomics Core Facility, University of Gothenburg (2)
Proteomics Core Facility, University of Gothenburg, Sweden (2)
University of Calgary (2)
(Monash University). Y. T. Candace Ho: yee.ho@monash.edu (Monash University) (1)
- Inst. of Neuroscience and Physiology, Dept. of Psychiatry and Neurochemistry, The Sahlgrenska Academy at University of Gothenburg, Mölndal, Sweden - Clinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden - Department of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London, UK (1)
1) Department Preclinical Development and Validation, Fraunhofer Institute for Cell Therapy and Immunology IZI, Leipzig, Germany; 2) Institute for Bioanalysis, University of Applied Science Coburg, Coburg, Germany (1)
1) OMICS and Analytical Development Group, BIOSCOPE Research Group, LAQV REQUIMTE, Chemistry Department, NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829-516, Caparica, Portugal (1)
1-University of Lille, CNRS, UAR 3290, MSAP, Miniaturisation pour la Synthèse l'Analyse et la Protéomique, F-59650 Villeneuve d’Ascq, France 2-Shrieking sixties, 1-3 Allée Lavoisier, F-59650 Villeneuve d'Ascq, France. (1)
1. Biomolecular Interactions, Max Planck Institute for Developmental Biology, Tübingen, Germany; 2. Applied Bioinformatics, Dept. of Computer Science, University of Tübingen, Germany; 3. Quantitative Biology Center (QBiC), University of Tübingen, Germany; 4. Institute for Translational Bioinformatics, University Hospital Tübingen, Germany; 5. Institute for Bioinformatics and Medical Informatics, University of Tübingen, Germany (1)
1. Department of Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany 2. Wellcome Trust Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom (1)
Applied Biosciences and Process Engineering, Anhalt University of Applied Sciences, Microbiology, Bernburger Straße 55, 06354 Köthen, Germany (1)
Applied Proteomics Lab, Department of Biology, Maynooth University, Co. Kildare, Ireland (1)
Beijing Proteome Research Center, 38 Science Park Road, Changping District, Beijing 102206, China. (1)
Bioinformatics Unit (MF 1), Department for Methods Development and Research Infrastructure, Robert Koch Institute, Berlin, Germany (1)
Biomarkers and Alternative Models Branch Division of Systems Biology National Center for Toxicological Research U.S. Food and Drug Administration 3900 NCTR Rd., HFT-233 Jefferson, AR 72079 USA (1)
Biomedical Engineering, Tufts University, Medford, MA (1)
Biomedicine Discovery Institute, Monash University, Clayton 3800, Victoria, Australia (1)
CSIR-Institute of Microbial Technology, Sector 39A, Chandigarh, India. (1)
CSIRO Agriculture and Food, 306 Carmody Rd, St Lucia QLD 4067, Australia (1)

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FAEVEr on biological fluids plasma and urine

Isolation of EVs from complex biofluids plasma and urine using the filter-aided EV enrichment strategy in combination with TWEEN-20 washes

ORGANISM(S): Homo sapiens (Human)

2025-05-07 | PXD056479 | Pride

FAEVEr 96well for high-throughput EV proteomics

Extracellular vesicles (EVs), nanoscale vesicles that are secreted by cells, are critical mediators for inter-cellular communication and play a crucial role in cancer development. As a result, EVs are regarded to have high potential value towards the clinic, both for diagnostic and therapeutic appli...

ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human)

2025-07-10 | PXD059819 | Pride

Extracellular vesicles Tween-20 300 kda mwco filtration

Non-targeted multimodal metabolomics and lipidomics data from ovine rumen fluid fractions

From an animal production and health perspective, our understanding of the metabolites in ruminant biofluids, particularly rumen fluid across different host species is poorly understood. Metabolomics is a powerful and sensitive approach for investigating low molecular weight metabolite profiles p...

2021-08-23 | MTBLS1717 | MetaboLights

Taxon-specific toxicity and composition of venom produced by araneophagous white-tailed spiders (Lamponidae: Lampona sp.)

Prey-specialised spiders are adapted to capture specific prey items, including dangerous prey such as ants, termites or other spiders. It has been observed that the venoms of specialists are often prey-specific and less complex than those of generalists, but venom composition has not been studied in...

ORGANISM(S): Lampona murina

2023-02-08 | PXD033502 | Pride

Venom peptide toxin spider

Catalytic Ozonation of Pharmaceuticals Using CeO₂-CeTiO_x-Doped Crossflow Ultrafiltration Ceramic Membranes.

Not available

S-EPMC11243686 | biostudies-literature

Dual-Stage Cross-Flow Filtration: Integrated Capture and Purification of Virus-Like Particles.

Not available

S-EPMC11895408 | biostudies-literature

Proteomics characterization of extracellular vesicles derived from fermented food industry by-product: looking for new potential delivery vectors

In the last decade, the interest in extracellular vesicles (EVs) as safe and biocompatible nano-transporters has risen dramatically, as these nanoparticles can be used to increase the delivery efficiency rate and reduce secondary effects. However, the difficulty for its obtention in large quantities...

ORGANISM(S): Bos taurus (Bovine)

2022-04-27 | PXD025780 | Pride

Food industry by-products Proteomics Evs Nanotransporters Nanovectors Molecular weight cut-off Lc-ms Extracellular vesicles Food-derived vesicles Circular economy

TAP-GluN1, PSD95-TAP, WT (control) BNP-LC-MS/MS proteomics

TAP-GluN1 (840 kDa and 1.5 MDa), PSD95-TAP (1.5 MDa) and WT (control; 1.5 MDa) native complexes from Grin1^TAP/TAP, Dlg4^TAP/TAP, and WT mouse forebrain (cortex and hippocampus), respectively. Purified samples were seperated by blue native PAGE. Bands were excised, digested with trypsin. Peptides we...

ORGANISM(S): Mus musculus (Mouse)

2016-04-20 | PXD000011 | Pride

Native complexes Synapse Nmdar

Improved Profiling of Low Molecular Weight Serum Proteome for Gastric Carcinoma by Data-independent Acquisition

Low molecular weight proteins (LMWPs) in the bloodstream participate in various biological processes and are closely associated with disease status, whereas identification of serous LMWPs remains a great technical challenge due to the wide dynamic range of protein components. In this study, we const...

ORGANISM(S): Homo sapiens (Human)

2022-07-11 | PXD034184 | Pride

Mass spectrometer Quantitative proteomics Data-independent acquisition (dia) Low molecular weight proteins (lmwps) Gastric carcinoma (gc)

Understanding condensation domain selectivity in non-ribosomal peptide biosynthesis: structural characterization of the acceptor bound state

Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)...

ORGANISM(S): Escherichia coli

2021-05-28 | PXD024004 | Pride

Non-ribosomal peptide biosynthesis condensation domain peptidyl carrier protein biocatalysis

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