{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7"],"submitter":["Winnicki W"],"pubmed_abstract":["<h4>Background</h4>Complement factor C3 represents the central component of the complement cascade and its activation split product C3a plays an important role in inflammation and disease. Many human disorders are linked to dysregulation of the complement system and alteration in interaction molecules. Therefore, various therapeutic approaches to act on the complement system have been initiated.<h4>Methods and results</h4>Aiming to develop a tool to eliminate C3a/C3 from the circulation, in a first step a high affine murine monoclonal antibody (mAb) (3F7E2-mAb) was generated against complement factor C3 and selected for binding to the C3a region to serve as immunoaffinity reagent. Functional testing of the 3F7E2-mAb revealed an inhibition of Zymosan-induced cleavage of C3a from C3. Subsequ"],"journal":["PeerJ"],"pagination":["e8218"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6921979"],"repository":["biostudies-literature"],"pubmed_title":["A novel approach to immunoapheresis of C3a/C3 and proteomic identification of associates."],"pmcid":["PMC6921979"],"pubmed_authors":["Sengolge G","Winnicki W","Beilhack G","Knafl D","Steinmacher I","Wagner L","Pichler P","Mechtler K","Imre R"],"additional_accession":[]},"is_claimable":false,"name":"A novel approach to immunoapheresis of C3a/C3 and proteomic identification of associates.","description":"<h4>Background</h4>Complement factor C3 represents the central component of the complement cascade and its activation split product C3a plays an important role in inflammation and disease. Many human disorders are linked to dysregulation of the complement system and alteration in interaction molecules. Therefore, various therapeutic approaches to act on the complement system have been initiated.<h4>Methods and results</h4>Aiming to develop a tool to eliminate C3a/C3 from the circulation, in a first step a high affine murine monoclonal antibody (mAb) (3F7E2-mAb) was generated against complement factor C3 and selected for binding to the C3a region to serve as immunoaffinity reagent. Functional testing of the 3F7E2-mAb revealed an inhibition of Zymosan-induced cleavage of C3a from C3. Subsequ","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019","modification":"2026-05-04T07:21:45.603Z","creation":"2026-04-07T20:15:48.54Z"},"accession":"S-EPMC6921979","cross_references":{"pubmed":["31871840"],"doi":["10.7717/peerj.8218"]}}