Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Flag-GABPα overexpression HEK293T cells LC-MS/MS

ABSTRACT: Immunoprecipitated by Flag and IgG antibody for protein capture by LC-MS/MS in HEK293T cells infected with GABPα-Flag overexpression plasmid.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Qianqian Kang

LAB HEAD: Yong Chen

PROVIDER: PXD070466 | Pride | 2026-02-23

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Flag.raw	Raw
	IgG.raw	Raw
	allPeptides.txt	Txt
	checksum.txt	Txt
	evidence.txt	Txt

Items per page:

1 - 5 of 18

Publications

Gabpα-Pparγ Complex Determines Glycolytic Capacity and Lactic Acid Homeostasis in Brown Fat.

Wang Zhihan Z Wang Huanyu H Kang Qianqian Q Pan Ruping R He Rui R Yang Min M Liu Jiadai J Peng Xuemin X Xie Yuyu Y Deng Hongyan H Wang Wenshe W Zhu Zengzhe Z Ge Jing J Liu Yulian Y Gao Ronghui R Guo Yaming Y Yu Peng P Pan Limeng L Li Danpei D Maretich Pema P Luo Xiaoping X Yu Xuefeng X Chen Yong Y

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 20251123 8

Glycolysis in brown adipose tissue (BAT) plays a critical role in fueling thermogenesis. However, the transcriptional control of glycolysis in brown fat remains poorly understood. Here, GA binding protein alpha chain (Gabpα) is identified as a key transcriptional regulator that sustains the glycolytic capacity of brown adipocytes. Gabpα is preferentially expressed in BAT, yet BAT-specific ablation of Gabpα substantially impairs glycolytic flux and heat production, leading to reduced glucose tole ...[more]

PMID: 41276932

Similar Datasets

FLAG-tagged FOXM1A Plasmid

Project description:FLAG-tagged FOXM1A Plasmid

| PRJEB24606 | ENA

Human Flag-tagged RIG-I IP-MS in HEK293T

Project description:nevaeh: The PARP inhibitor olaparib is widely used in cancer but is underused in treating lung adenocarcinoma (LUAD). Our initial analysis revealed that RIG-I, which is typically found in the cytoplasm and activates innate immunity, is linked to LUAD outcome. Here, we discovered that RIG-I undergoes lactylation, with the acetyltransferase PCAF serving as the lactylation writer. Treatment with the lactate transporter inhibitor syrosingopine prevents the efflux of lactic acid from cancer cells, increasing intracellular lactic acid, promoting RIG-I lactylation, and enhancing its interaction with the nuclear transport protein importin 8. The augmented interaction facilitates the nuclear translocation of RIG-I, diminishing PARP1 activity and enhancing the therapeutic effects when combined with olaparib. This synergy disrupts PARP1-mediated DNA repair mechanisms, increasing drug sensitivity and inhibiting tumor growth. The combination of olaparib and syrosingopine demonstrates better therapeutic efficacy than olaparib monotherapy in LUAD, providing a promising strategy for future LUAD treatments. nevaeh: HEK293T cells were transfected with Flag-RIG-I for 48 h, lysed in NP-40 buffer, and sonicated using a JY92-II sonicator. The supernatant was first incubated overnight with an anti-Flag conjugated with beads (Sigma, A2220) after being denatured. Following centrifugation at 3,000 rpm (4°C for 5 min), the supernatants were completely removed, and 60 μL of Flag–peptide was added to competitively bind to the beads. RIG-I protein was released, precipitated using Trichloroacetic acid (TCA), and subjected to mass spectrometry analysis for lactylation.

2025-12-10 | PXD058597 | Pride

JOSD2 inhibits angiotensin II-induced vascular remodeling by deubiquitinating and stabilizing SMAD7

Project description:Increased level of angiotensin II (Ang II) plays a central role in the development of hypertensive vascular remodeling. Here, we identify the deubiquitinating enzyme JOSD2 as a protective factor and investigate its molecular mechanism in Ang II-induced vascular remodeling. Firstly, we found that JOSD2 was up-regulated in aortic smooth muscle cells but not endothelial cells of Ang II-challenged mouse vascular tissues. Whole-body knockout of JOSD2 significantly deteriorated Ang II-induced vascular remodeling in mice. Conversely, Ang II-induced vascular remodeling was reversed by VSMC-specific JOSD2 overexpression. In vitro, JOSD2 deficiency aggravated the fibrosis, proliferation, and migration induced by Ang II in vascular smooth muscle cells (VSMCs), while these changes were reversed by JOSD2 overexpression. RNA-seq analysis showed that the protective effects of JOSD2 in VSMCs were related to TGFβ-SMAD pathway. Furthermore, the LC-MS/MS analysis identified SMAD7, a negative regulator in TGFβ-SMAD pathway, as the substrate of JOSD2. JOSD2 specifically bound to the MH1 domain of SMAD7 to removed K48-linked Ub chains of SMAD7 at lysine 220 to sustain SMAD7 stability. Taken together, our finding reveals that JOSD2-SMAD7 axis is critical for relieving Ang II-induced vascular remodeling and JOSD2 maybe a novel and potential therapeutic target for hypertensive vascular remodeling.

2024-10-10 | PXD056674 | Pride

ChIP-seq of PtrVCS2 fuse FLAG overexpression plants

Project description:ChIP-seq was carried out with FLAG antibody using stem cambium tissues from PtrVCS2-FLAG overexpression plants

2022-11-11 | GSE201005 | GEO

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 Kidney Cells(293T-Vector/Flag-△50),LC-MSMS

Project description:Hutchinson-Gilford progeria syndrome (HGPS) is a premature aging disease caused by progerin accumulation. However, the mechanism of how progerin causes cell defects is unclear in HGPS cells. To further investigate the possible mechanism, we used Flag-tagged progerin as bait in mass spectrometry to survey the possible regulatory factors.

2023-01-30 | PXD039136 | Pride

Identification of OsSGS3a-FLAG-interacting proteins by IP-MS/MS

Project description:OsSGS3a-FLAG and its interacting proteins were enriched by immunoprecipitation using Anti-FLAG M2 Magnetic Beads. Then, OsSGS3a-FLAG-interacting proteins were identified by mass spectrum.

2023-08-02 | PXD043706 | Pride

Pull-downs of non-crosslinked or in-cell SDA crosslinked FLAG-AK2-transfected 293 cells

Project description:Human cells were transfected with a plasmid encoding FLAG-AK2 and subsequently treated with a photoactivatable crosslinker, SDA, or left untreated. Pulldowns were performed from these cells, and the bead-bound material was digested and subjected to LC-MS DIA runs for analysis.

2025-05-06 | PXD052867 | Pride

iCLIP of FLAG-PURA overexpression with anti-FLAG antibody in HeLa cells

Project description:iCLIP of FLAG-PURA overexpression with anti-FLAG antibody in HeLa cells

| PRJNA798375 | ENA

MS-based sequencing of the anti-FLAG-M2 antibody

Project description:We demonstrate a method for direct de novo sequencing of monoclonal IgG from the purified antibody products. The method uses a panel of multiple complementary proteases to generate suitable peptides for de novo sequencing by LC-MS/MS in a bottom-up fashion. Furthermore, we apply a dual fragmentation scheme, using both stepped high-energy collision dissociation (stepped HCD) and electron transfer high-energy collision dissociation (EThcD) on all peptide precursors. The method achieves full sequence coverage of the monoclonal antibody Herceptin, with an accuracy of 98% in the variable regions. We applied the method to sequence the widely used anti-FLAG-M2 mouse monoclonal antibody, which we successfully validated by remodeling a high-resolution crystal structure of the Fab and demonstrating binding to a FLAG-tagged target protein in Western blot analysis. The method thus offers robust and reliable sequences of monoclonal antibodies.

2021-01-11 | PXD023419 | Pride

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