Project description:To further illustrate the mechanism of HEXB mediated YAP1 activation in GBM cells, immunoprecipitation-mass spectrometry (IP-MS) was employed to identify potential binding partners of HEXB.
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.
Project description:HA-LUBEL 1-872 or LacZ (control) was expressed under the control of Mef2-GAL4, and the progenies were raised at 25°C. The 3IL carcass fillet lysates were subjected to anti-HA immunoprecipitation. To identify potential binding partners, we performed immunoprecipitation-mass spectrometry (IP-MS) of LUBEL1-872.
Project description:To elucidate the molecular mechanisms by which GPX4 regulates mitochondrial function, we overexpressed GPX4 in cardiomyocytes and subjected them to hypoxia-reoxygenation (H/R) modeling. Co-immunoprecipitation (Co-IP) coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) was employed to identify potential partners of GPX4.
Project description:We screened the protein partners that associate with CHRONO using immunoprecipitation followed with mass spectrometry (IP-MS). IP-MS identified proteins involved in multiple protein-protein interaction networks that are functional in multiple pathways and cellular functions.
Project description:With the aim of revealing potential conserved or novel regulatory partners that could explain the phenotypes present on plant cells expressing p53, we performed p53-immunoprecipitation in combination with mass spectrometry (IP-MS) on 3-week-old XVE:p53 root cultures treated with DMSO (control) or 10µM ß-estradiol (inducer) for 24h.
Project description:To analyze OTX2 function in adult choroid plexus, we performed several OTX2 co-immunoprecipitation (co-IP) experiments with mass spectrometry analysis to identify potential protein partners. We previously discovered that OTX2 protein also accumulates non-cell autonomously in subventricular zone (SVZ) and rostral migratory stream (RMS) astrocytes and in visual cortex (VCx) parvalbumin cells. The identification of alternate protein partners in cell-autonomous and non-cell-autonomous contexts would suggest OTX2 takes on specific roles after transferring between cells. In order to test this hypothesis, and to reinforce choroid plexus analysis, we also performed OTX2 co-IP on lysates from adult mouse SVZ, RMS and VCx.
Project description:All raw files correspond to porcine kidney epithelial cell (PK15) samples, including two groups: one group named IP-SA14 was the cellular protein from PK15 cell infected with JEV. The other group named IP-kong was control group from normally cultured PK15 cells. all raw spectral data are integrated into one summary identification search result quantification excel table for Partial deposition. This dataset was generated by immunoprecipitation (IP) combined with LC-MS/MS to investigate host proteins interactin with JEV Envelop protein in PK15 cell. PK15 cells were infected with JEV at an MOI of 1, and cell lysates were collected at 24 hpi. Proteins Immunoprecipitation using the TAKARA Capturem™ IP & Co-IP Kit (Takara/Clontech, 635721). And the antibody against the JEV E protein was used to capture endogenous protein complexes, followed by quantitative proteomic analysis to screen interactive protein partners between cellular protein and Japanese encephalitis virus. All raw Thermo RAW files and complete quantitative excel table are deposited via Partial submission.
Project description:SORL1 (Sortilin-Related Receptor 1) is a key player in endosomal trafficking and has been implicated in neurodegenerative disorders. To identify SORL1 binding partners, we performed immunoprecipitation (IP) of SORL1, followed by mass spectrometry-based proteomic analysis. THP-1 cell lysates were used as the source material for immunoprecipitation, and IgG controls were included to filter out non-specific interactions. The resulting datasets provide insights into SORL1-associated protein complexes, offering potential targets for further functional studies.