MassIVEapplication/xmlftp://massive-ftp.ucsd.edu/v12/MSV000100816/primaryOK200ProteomicsErick Jose Ramo da SilvaBeatriz Rezende SantosNoemia Aparecida Partelli MarianiLucilene Delazari dos SantosOrbitrap Fusion LumosHomo Sapiens (ncbitaxon:9606)https://massive.ucsd.edu/ProteoSAFe/dataset.jsp?task=4e4ee64d801a417eaaca1a6d6861219aInstitute of Biosciences (UNESP), BotucatuInstitute of Biotechnology (UNESP), Botucatunoemia.partelli@unesp.brbeatriz.rezende@unesp.brejr.silva@unesp.brlucilene.delazari@unesp.brMassIVE17UNIMOD:4 - "Iodoacetamide derivative."UNIMOD:35 - "Oxidation or Hydroxylation."falseProteomic Analysis of EPPIN Interacting Proteins in Human Spermatozoa Identified by Co Immunoprecipitation Followed by Mass Spectrometry Epididymal Protease Inhibitor (EPPIN) is a sperm-associated protein that serves as a docking site for protein protein interactions. Its binding to seminal plasma proteins plays a key role in modulating sperm function. However, the molecular mechanisms underlying these roles remain unclear. This dataset contains proteomic profiles of proteins from human ejaculated spermatozoa that were immunoprecipitated using an anti EPPIN antibody and analyzed by mass spectrometry. This study aimed to characterize proteins associated with EPPIN in human spermatozoa, with a focus on identifying potential partners related to sperm function within intracellular compartments. Thu Feb 12 03:16:00 GMT 2026MSV000100816