Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Gene expression profile at single cell level of cultuted bovine milk-derived cells (MiDCs)

ABSTRACT: Gene expression profile at single cell level of cultuted bovine milk-derived cells (MiDCs)

PROVIDER: PRJNA956553 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR24196182.fastq.gz	Fastqsanger.gz
	SRR24196183.fastq.gz	Fastqsanger.gz

Items per page:

1 - 2 of 2

Similar Datasets

Gene expression profile at single cell level of cultuted bovine milk-derived cells (MiDCs)

Project description:Bovine milk derived cells are a novel population with reported stem cell-like properties. We assessed these cells using scRNA-seq for markers of pluripotency and other features associated with the effects of their conditioned medium (CM).

2023-08-03 | GSE229898 | GEO

Proteomic analysis of bovine milk-derived extracellular vesicles isolated via salting-out

Project description:We developed a novel and cost-effective procedure to separate bovine milk-derived extracellular vesicles via salting-out and aimed to profile their proteomics as one important characterization in EV research.

2021-11-02 | PXD028095 | Pride

Bovine milk

Project description:Bovine milk Metagenome

| PRJNA529353 | ENA

Bovine milk

Project description:Bovine milk Metagenomic assembly

| PRJNA667207 | ENA

Antibody-independent identification of bovine milk-derived peptides in breast-milk

Project description:Exclusively breast-fed infants can exhibit clear signs of IgE or non IgE-mediated cow’s milk allergy. The definite characterization of dietary cow’s milk proteins (CMP) that survive the maternal digestive tract to be absorbed into the bloodstream and secreted into breast milk remains missing. The aim of this study was to assess the occurrence of CMP-derived peptides in breast milk, using antibody-independent methods. Using high performance liquid chromatography-high resolution mass spectrometry in blinded assays, we identified 11 cow’s milk-derived peptides, including two β-lactoglobulin (2 out 6 samples) and one αs1-casein (1 out 6 samples) fragments, in breast milk from mothers receiving a cup of bovine milk daily. The β-lactoglobulin (β-Lg) fragments, namely f42-54 and f42-57, were absent in milk from mothers who observed a strict dairy-free diet (6 samples). In contrast, neither intact nor hydrolyzed β-Lg was detected by Western blot or competitive ELISA tests. CMP-derived peptides rather than intact CMP may sensitize or elicit allergic responses in the neonate through mother’s milk. Immunologically active peptides from the maternal diet could be involved in priming the newborn’s immune system to drive tolerogenic response in neonates and infants.

2016-07-19 | PXD003657 | Pride

Functional profile of bovine blastocyst-derived trophoblasts

Project description:Functional profile of bovine blastocyst-derived trophoblast cells

2018-11-13 | MSV000083135 | MassIVE

Bovine Milk

Project description:Bovine Milk Raw sequence reads

| PRJNA509157 | ENA

Delineating Bovine Milk Derived Microvesicles from Exosomes Using Proteomics

Project description:This is a dataset for a publication in revision for the Journal of Proteome Research titled "Delineating Bovine Milk Derived Microvesicles from Exosomes Using Proteomics". The paper explores the extracellular vesicle proteomics of bovine milk treated with a serial ultracentrifugation method that partially separates differently sized particles. We used a clustering method to group proteins with corresponding categories of particles.

2024-02-02 | MSV000093982 | MassIVE

Protein profiling of bovine colostrum and transition milk

Project description:The protein profile of bovine milk serum was characterised as milk transitions from colostrum to transition milk over the first 5 days of lactation. Samples were collected from first and third parity cows at days 0, 2, 5 (D0, D2, D5) after calving. Following isolation of the milk serum fraction, label-free quantitative proteomics was carried out following normalisation by total protein concentration. Protein profiles indicated samples clustered by day postpartum, but not by parity. Proteins (n = 471) were identified and relative quantification was performed, with 199 protein groups showing altered abundance by day of lactation (fold change ≥ 2, P < 0.05). Elevated levels of immune proteins, including immunoglobulins and complement proteins were detected in colostrum with levels significantly decreasing by D2. These findings provide an outline of the dynamics of the protein profile of bovine milk and colostrum in early lactation.

2023-09-25 | PXD044877 | Pride

Antibody-independent identification of bovine milk-derived peptides in breast-milk

Project description:Exclusively breast-fed infants can exhibit clear signs of IgE or non IgE-mediated cow’s milk allergy. The definite characterization of dietary cow’s milk proteins (CMP) that survive the maternal digestive tract to be absorbed into the bloodstream and secreted into breast milk remains missing. The aim of this study was to assess the occurrence of CMP-derived peptides in breast milk, using antibody-independent methods. Using high performance liquid chromatography-high resolution mass spectrometry in blinded assays, we identified 11 cow’s milk-derived peptides, including two ?-lactoglobulin (2 out 6 samples) and one ?s1-casein (1 out 6 samples) fragments, in breast milk from mothers receiving a cup of bovine milk daily. The ?-lactoglobulin (?-Lg) fragments, namely f42-54 and f42-57, were absent in milk from mothers who observed a strict dairy-free diet (6 samples). In contrast, neither intact nor hydrolyzed ?-Lg was detected by Western blot or competitive ELISA tests. CMP-derived peptides rather than intact CMP may sensitize or elicit allergic responses in the neonate through mother’s milk. Immunologically active peptides from the maternal diet could be involved in priming the newborn’s immune system to drive tolerogenic response in neonates and infants.

2017-04-02 | MSV000080880 | MassIVE

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data