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Following centrifugation at 11,000xg to pellet debris, protein from whole cell lysates (WCL) were quantified using the BioRad protein quantitation assay (Bio-Rad, #5000006) and measured on a Cytation 3 (BioTek) plate reader using known BSA serial dilutions as a standard curve at 595nm (colorimetric). 430μg of protein WCL were used for each set of immunoprecipitations and were diluted to 165uL in PBST (PBS + 0.01% Tween-20). 100μL of Protein-G Dynabeads (Thermo) were washed with Citrate Phosphate Buffer (25mM citric acid, 50mM dibasic sodium phosphate dihydrate in H2O calibrated to pH5.0) twice followed by resuspension in 260uL of PBST. Diluted WCL were then pre-cleared to remove proteins that non-specifically bind to Protein-G Dynabeads by adding 55uL of washed beads to the diluted WCL and incubating them at 4C for 1hr on a rotator, followed by transfer of the pre-cleared eluate to a new tube. 2μg of antibodies (DPPA2 (Mouse); Sigma #MAB4356, DPPA4 (Rabbit); abcam #ab154642) or IgG’s isotype controls (Mouse; Invitrogen #31903, Rabbit; Invitrogen #02-6102) diluted to 150uL in PBST were conjugated to 50uL of washed beads by incubating them together at 4C for 1hr on a rotator. Antibody-bead conjugates were washed two times with PBST and then resuspended in 55uL PBST. Immunoprecipitations were then performed by incubating 50uL of antibody-bead conjugates with 50uL of pre-cleared WCL overnight at 4C whilst rotating, the rest of the pre-cleared WCL was kept as an input control. Following immunoprecipitation, beads were washed five times with PBS on ice, and beads were snap frozen on dry ice as a pellet for eventual on-bead tryptic digest for mass spectrometry. Enriched proteins were digested off the beads overnight at 37C in 50uL of 2M urea containing 1mM tris(2-carboxyethyl)phosphine and 4mM 2-chloroacetamide with 0.4ug of sequencing grade trypsin (Promega, #V5280) and LysC (Wako, #125-05061). The peptides were purified using SDB-RPS microcolumns, washed with 99% isopropanol containing 1% trifluoracetic acid (TFA) followed by 5% acetonitrile containing 1% TFA and the eluted with 80% acetonitrile containing 1% ammonium hydroxide. Peptides were dried by vacuum centrifugation and resuspended in 2% acetonitrile containing 0.1% TFA. Peptides were separated on a Dionex 3500 nanoUHPLC, coupled to an Orbitrap Lumos mass spectrometer via electrospray ionization in positive mode with 1.9 kV at 275 °C and RF set to 30%. Separation is achieved on a 50 cm × 75 µm column packed with C18AQ (1.9 µm) over 40 min at a flow rate of 300 nL/min. Peptides were eluted over a linear gradient of 3–40% Buffer B (Buffer A: 0.1% v/v formic acid; Buffer B: 80% v/v acetonitrile, 0.1% v/v FA) and the column was maintained at 50°C. The instrument was operated in data-independent acquisition (DIA) mode, with an MS1 spectrum acquired over the mass range 350–1,400 m/z (60,000 resolution, 100% automatic gain control (AGC), and 45 ms maximum injection time) followed by sequential MS/MS spectra across 13.7 m/z isolation windows with 1 m/z overlap covering the full mass range. MS/MS data will be acquired with higher-energy collisional dissociation (HCD) fragmentation (15,000 resolution, 2000% AGC, 55 ms maximum injection time, and normalized collision energy 30%)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Data were processed in Spectronaut 1 (v7.6.230428.55965) with default setting against the Homo sapien protein FASTA sequences in the Uniprot database and filtered to 1% FDR at the PSM, peptide and protein level. Raw label-free quantitation values (LFQ-AUC) values were subject to down-shifted imputation, whereby missing values for a given protein were imputed with a low intensity LFQ-AUC value based on the normalised distribution of the dataset. Following imputation, LFQ-AUC values were centered for each protein by log2 transformation and subtraction of the median across all samples. To determine enrichment statistics, unpaired Student's t-tests were performed between the IP conditions (DPPA2, DPPA4) and matched control IgG (Ms, Rb) respectively, followed by p-value adjustment to account for multiple comparisons using the Benjamini-Hochberg method."],"omics_type":["Proteomics"],"labhead":["Melanie Eckersley-Maslin"],"instrument_platform":[""],"labhead_affiliation":["Peter MacCallum Cancer Centre, Melbourne, Australia Department of Anatomy and Physiology, The University of Melbourne, Melbourne, VIC, Australia"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["janith.seneviratne@petermac.org"],"publication":["41862192 Seneviratne JA, Crisp CL, Glancy E, Choy N, Tan W, Neve M, Stammers M, Wang T, Johnstone R, Kaur A, Fennell KA, Burr ML, Parker BL, Shakeel S, Eckersley-Maslin MA. Embryonic stem cell factors DPPA2/4 amplify active H3K4me3-H2AK119ub chromatin domains in non-small cell lung cancer. Genes Dev. 2026 10.1101/gad.353102.125"],"submitter_affiliation":["Peter MacCallum Cancer Centre"],"submitter_country":["Australia"],"additional_accession":[]},"is_claimable":false,"name":"Human non-small cell lung cancer cell line NCI-H661 DPPA2-4 immunoprecipitation mass spectrometry (LC-MSMS)","description":"We performed endogenous DPPA2/4 immunoprecipitations from whole cell lysates of the human non-small cell lung cancer cell line NCI-H661, followed by LC-MS/MS to identify enriched 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