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• W1505657283 endingPage "2715" @default.
• W1505657283 startingPage "2708" @default.
• W1505657283 abstract "The identification of all CD28/CTLA-4 counterreceptors is critical to our understanding of this pivotal pathway of T cell activation. Clouding our understanding has been the reported discrepancies in expression and function of the B7-1 (CD80) molecule based upon the use of the BB1 vs other anti-B7-1 mAbs. To resolve this issue, we have cloned a BB1-binding molecule from the BB1+B7-1(-) NALM-6 pre-B cell line. Here, we demonstrate that this BB1-binding molecule is identical to the cell surface form of CD74 (MHC class II-associated invariant chain). CD74-transfected cells bound the BB1 mAb but not other anti-CD80 mAbs, CD28-Ig, or CTLA4Ig. Absorption and blocking experiments confirmed the reactivity of BB1 mAb with CD74. A region of weak homology was identified between CD74 and the region of B7-1 encoding the BB1 epitope. Therefore, the BB1 mAb binds to a protein distinct from B7-1, and this epitope is also present on the B7-1 protein. Many of the puzzling observations in the literature concerning the expression of human B7-1 are resolved by an understanding that BB1 staining is the summation of CD74 plus B7-1 expression. This observation requires the field to reconsider studies using BB1 mAb in the analysis of CD80 expression and function." @default.
• W1505657283 created "2016-06-24" @default.
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• W1505657283 date "1998-09-15" @default.
• W1505657283 modified "2023-10-10" @default.
• W1505657283 title "The BB1 Monoclonal Antibody Recognizes Both Cell Surface CD74 (MHC Class II-Associated Invariant Chain) as Well as B7-1 (CD80), Resolving the Question Regarding a Third CD28/CTLA-4 Counterreceptor" @default.
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• W1505657283 doi "https://doi.org/10.4049/jimmunol.161.6.2708" @default.
• W1505657283 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9743327" @default.
• W1505657283 hasPublicationYear "1998" @default.
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