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ProteomicsCMK LC-MS/MS after CoIP of ARID3A
In order to determine proteins interacting with ARID3A in the ML-DS cell line CMK, we performed CoIP of endogenous ARID3A followed by LC-MS/MS
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD025027 | Pride
Cmk Arid3a Ml-ds 
ProteomicsC1QBP mitochondrial interactome
The study of protein-protein interactions is an essential process to understand the biological functions of proteins and the underlying mechanisms. Co-immunoprecipitation coupled with mass spectrometry (CoIP-MS) is one of the most extensively used high-throughput techniques to discover novel protein...
ORGANISM(S): Homo Sapiens 
2015-11-04 | MSV000079369 | MassIVE
ProteomicsIdentification of GltB-interacting proteins by CoIP-MS
To investigate whether GltB possess more function, Co-immunoprecipitation coupled with Mass Spectrometry (CoIP-MS) was used to isolate the putative GltB binding proteins.We used strains PAO1/p-gtrS-YFP and ΔgltB/p-gtrS-YFP to ensure the membrane protein GtrS of great interest is at high levels. A ta...
ORGANISM(S): Pseudomonas aeruginosa PAO1 
2021-09-09 | PXD020213 | Pride
Pseudomonas aeruginosa Gltb-interacting protein Lc-ms/ms 
ProteomicsCoIP-MS based method to identify FNIP1 binding proteins in exercising muscle
Using muscle-specific FNIP1 (WT) and FNIP1 (S220A Tg) muscle tissues, we identified approximately 600 potential FNIP1 (WT) or FNIP1 (S220A) binding proteins in exercising muscle tissue of the corresponding mice by the CoIP-MS method, proteomic analysis showed that both FNIP1 (WT) and FNIP1 (S220A) i...
ORGANISM(S): Mus musculus (Mouse) 
2023-11-17 | PXD046977 | Pride
Mouse Coip. Muscle 
ProteomicsHuman SUMOylated Golgin45 CoIP-MS
HeLa cells expressing mCherry-Golgin45, Flag-UBC9-WT/DN and myc-SUMO1 were subjected to Co-IP experiment using RFP-beads (M165-8, MBL life science). Independent triplicates of mCherry-Golgin45 Co-IP experiments were prepared and analyzed by MS independently in a label free format.
ORGANISM(S): Homo sapiens (Human) 
2024-06-23 | PXD051237 | Pride
Human Coip-ms Golgin45 Sumoylation 
ProteomicsRNA polymerase III (Pol III) CoIP ms/ms
RNA polymerase III (Pol III) synthesizes noncoding RNAs essential for translation, RNA processing, transcription regulation, and other core cellular processes. Pol III transcription levels are coordinated with nutrient availability for cellular growth, and its dysregulation is linked to disease, suc...
ORGANISM(S): Homo sapiens (Human) 
2026-09-03 | PXD061197 | Pride
Human Coip ms/ms Rna polymerase iii 
ProteomicsGrass carp SERPINA1 CoIP with hepatopancreas mass spectrometry analysis
SERPINA1, a member of the serine protease inhibitor family, plays a role in viral infection and inflammation by regulating the activities of serine and cysteine proteases. To further investigate the antiviral role SERPINA1 played in GCRV (Grass carp Reovirus) infection, a polyclonal antibody of SERP...
ORGANISM(S): Ctenopharyngodon idella 
2022-08-31 | PXD036356 | Pride
Serpina1 Grass carp Coip/ms Hepatopancreas 
ProteomicsLC-MS/MS analysis: coIP of Tssc4-Flag from nuclear extracts of HEK293 cells
Interactome analysis of human Flag-tagged Tssc4, Tssc4 mutant and background control. The coIP's (n=3) were performed from nucelar extract of HEK293 cells followed by LC-ESI-MS/MS analysis.
ORGANISM(S): Homo sapiens (Human) 
2022-01-17 | PXD029493 | Pride
Lc-ms/ms coip 
ProteomicsProtein co-immmunoprecipitation using antibodies specific for the antimicrobial peptide FsPDF2 from Fagus sylvatica
To assess the specificity of the antibodies used in the quantitative sandwich ELISA, co-immunoprecipitation (CoIP) was performed. Proteins binding to these antibodies were detected using LC-MS/MS in DDA mode.
ORGANISM(S): Fagus sylvatica 
2026-06-08 | PXD060631 | Pride
Co- immunoprecipitation (coip) Antimicrobial peptides Fagus sylvatica 
ProteomicsInteraction partners of arginyl-tRNA protein transferase in the moss Physcomitrella patens
Protein arginylation is a post-translational modification at the N-terminus of proteins and is crucial for viability and physiology in higher eukaryotes. The lack of arginylation causes severe developmental defects in plants and embryo lethality in Drosophila and in mice. Although several studies in...
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2016-04-19 | PXD003228 | Pride
Moss Protein interaction Co-ip Physcomitrella patens Lc-ms/ms 
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