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Anion Exchange Chromatography-Based Purification of Exosomes from Beta Vulgaris.

ABSTRACT: A purification platform that integrates ultrafiltration (UF) with anion exchange chromatography in a fast protein liquid chromatography (FPLC) system, which provides superior resolution, reproducibility, and automation, making it an ideal choice for scaling up exosome isolation from Beta Vulgaris.

INSTRUMENT(S):

ORGANISM(S): Beta Vulgaris (sugar Beet)

TISSUE(S): Leaf

SUBMITTER: Simona Arena

LAB HEAD: Andrea Scaloni

PROVIDER: PXD068478 | Pride | 2025-12-22

REPOSITORIES: Pride

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			Action	DRS
	RAPA1.raw	Raw
	RAPA10.raw	Raw
	RAPA10_20240409150700.raw	Raw
	RAPA11.raw	Raw
	RAPA11_20240409160802.raw	Raw

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1 - 5 of 31

Publications

Isolation of Red Beet Plant-Derived Nanovesicles, and Characterization of Their Molecular Content and Biological Activities in Human Cells.

Zanotti Clarissa C Troise Antonio Dario AD Arena Simona S Renzone Giovanni G De Pascale Sabrina S Ferracane Rosalia R Pontecorvi Chiara C Niespolo Chiara C Gismondi Angelo A Scaloni Andrea A Marra Mauro M

International journal of molecular sciences 20251121 23

Nowadays, growing evidence indicates that plant-derived nanovesicles cross biological barriers between species, including humans, and deliver therapeutic molecules that influence gene expression, affecting various processes such as inflammation, oxidative stress, and cancer. For these reasons, plant-derived nanovesicles are gaining attention as a valuable substitute for mammalian exosomes as they offer benefits such as reduced immunogenicity, enhanced bioavailability, and the inclusion of benefi ...[more]

PMID: 41373418

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Anion Exchange Chromatography-Based Purification of Exosomes from Brassica oleracea L.

Project description:A purification platform that integrates ultrafiltration (UF) with anion exchange chromatography in a fast protein liquid chromatography (FPLC) system, which provides superior resolution, reproducibility, and automation, making it an ideal choice for scaling up exosome isolation.

2025-08-25 | PXD063392 | Pride

2E7 Antigen Identification Using PhAbomics Technology

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2025-11-20 | PXD065365 | Pride

USP26 overexpressing HEK293T cells LC-MS/MS

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2024-09-09 | PXD051958 | Pride

Mapping the Interactome of KRAS and Its G12C/D/V Mutants by Integrating TurboID Proximity Labeling with Quantitative Proteomics

Project description:RAS is one of the most frequently mutated proto-oncogenes in human malignancies, with mutation sites and subtypes exhibiting tumor-type dependent distribution. Oncogenic RAS mutations will maintain continuously GTP-bound activation states that leading to dysregulation of downstream signaling, ultimately disrupting cellular homeostasis to induce malignant transformation of cells. In this study, we employed TurboID proximity-labeling technology integrated with quantitative proteomics LC-MS/MS to systematically characterize the proximal binding proteins of wild-type KRAS and three high-frequency oncogenic mutant subtypes G12C, G12D and G12V. Through comprehensive bioinformatic analysis of mutation-specific interaction networks and distinct metabolic pathways, we identified significant enrichment of mutant KRAS binding proteins in insulin signaling pathway, reactive oxygen species related pathways, glucose and lipid metabolism and so on. Metabolic reprogramming pathways in KRAS G12 mutations collectively fuel tumor proliferation and immune evasion. In addition, we also comparatively analyzed the proximal binding proteins similarity in three G12 mutants. Notably, we observed that the KRAS E3 ubiquitin ligase adaptor LZTR1 diminished binding with mutations, and the mTORC1 important regulatory protein LAMTOR1 was enhanced recruitment by mutations. This multi-dimensional profiling delineates a comprehensive mapping of KRAS WT and G12 mutant interactomes and unveils the metabolic reprogramming pathways associated with KRAS activating mutations. Our analysis result provides potential therapeutic targets for KRAS-driven tumorigenesis while establishing a mechanistic framework for developing KRAS mutation-specific therapeutic strategies.

2025-06-09 | PXD062101 | Pride

Ribosome dynamics orchestrate mRNA stability and translation across natural and synthetic systems

Project description:The dynamic interplay between ribosomes and mRNAs plays a central role in gene expression regulation, balancing protein synthesis and mRNA stability. However, traditional methods capturing static ribosome occupancy fail to resolve the temporal dynamics governing these processes. Here, we introduce Temporal Ribosome Density Profiling (TRiP), which combines metabolic RNA labeling and polysome sequencing to map ribosome density dynamics across the mRNA lifespan. TRiP reveals a striking temporal symmetry conserved across cell types: gene-specific ribosome loading rates are counterbalanced by coordinated unloading rates, creating a self-regulatory loop that, as demonstrated through biophysical modeling and experimental validation in diverse cellular contexts, directly couples ribosome dynamics to mRNA stability. We further uncover how mRNA structural motifs and m6A methylation fine-tune ribosome dynamics at the isoform level, simultaneously modulating protein output and transcript half-life. In macrophages, this dynamic control enables rapid immune responses by upregulating translation efficiency of pro-inflammatory genes. Remarkably, these principles extend to synthetic mRNAs, where machine learning-guided optimization of ribosome dynamics enhances protein production. Our work establishes ribosome density dynamics as a pervasive and tunable regulatory axis, with broad implications for adaptive immunity, RNA biology, and the design of therapeutic mRNAs.

2025-12-10 | PXD070830 | Pride

THP-1 data for:Ribosome dynamics orchestrate mRNA stability and translation across natural and synthetic systems

2025-12-10 | PXD070845 | Pride

Hepa1-6 cell line overexpressing Flag-LTA4H LC-MS/MS

Project description:To explore potential proteins binding with LTA4H, co-immunoprecipitation (co-IP) and LC-MS/MS analysis were performed using Hepa1-6 cells overexpressing Flag-LTA4H. Anti-Flag and anti-IgG antibodies were used for immunoprecipitation to identify the interacting proteins.

2025-05-07 | PXD060326 | Pride

human Embryonic stem cells LC-MSMS

Project description:Genomic instability is the main cause of abnormal embryo development and abortion. NLRP7 dysfunctions affect embryonic development and lead to Hydatidiform Moles, but the underlying mechanisms remain largely elusive. Here, we show that NLRP7 knockout affects the genetic stability, resulting in increased DNA damage in both human embryonic stem cells and blastoids, making embryonic cells in blastoids more susceptible to apoptosis. Mechanistically, NLRP7 can interact with factors related to alternative splicing and DNA damage response, including DDX39B, PRPF8, THRAP3 and PARP1. Moreover, NLRP7 dysfunction leads to abnormal AS of genes involved in Homologous recombination in human embryonic stem cells, Such as Brca1 and Rad51. These results indicate that NLRP7-mediated Alternative splicing is potentially required for the maintenance of genome integrity during early human embryogenesis. Together, this study uncovers that NLRP7 plays an essential role in the maintenance of genetic stability during early human embryonic development by regulating alternative splicing of Homologous Recombination-related genes.

2025-01-17 | PXD059649 | Pride

Mass spectrometry identification of phosphorylation sites of GCN5 in rice

Project description:Firstly, wild type seedlings that had germinated in root tubes for 14 days were taken to prepare protoplasts. The GCN5-FLAG transient expression vector was transformed into wild type protoplasts. The protoplasts were collected and purified by Flag beads. After quality testing of the samples, phosphorylation mass spectrometry sequencing of GCN5 was performed.

2025-10-28 | PXD066361 | Pride

Identification of novel KRT32-associated proteins in primary keratinocytes cells lysate by GST-KRT32 pulldown assays coupled with mass spectrometry.

Project description:GST-KRT32 and its interacting proteins in primary keratinocytes cells were enriched by pull-down using glutathione-Sepharose beads. Then, KRT32-interacting proteins were identified by mass spectrum. Proteins obtained in Pulldown were subjected to SDS-PAGE gel electrophoresis and silver staining. The SDS-PAGE gel was sent to the mass spectrometry platform of the Jingjie PTM Biolab for subsequent processing and mass spectrometry detection.

2024-06-17 | PXD050141 | Pride

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