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• W2051233616 abstract "We report the generation of a monoclonal antibody (MAb) that reacts to the N-terminus of the denatured HLA-DRα chain. The 1C4.6 MAb was raised against a peptide corresponding to amino acid residues 10 to 32 of a highly conserved region within the α1 domain of HLA-DR. This region partially overlaps with the epitope recognized by the conformationally dependent L243 MAb. In Western blot analysis, MAb 1C4.6 reacted with denatured HLA-DRα chains, but failed to bind the HLA-DRβ chain expressed individually by transfectant cells, confirming that it recognizes an epitope on the α-chain of HLA-DR. In addition, this antibody was found to be isotype specific to HLA-DRα, as it did not cross-react to HLA class II proteins HLA-DP and-HLA-DQ. The 1C4.6 MAb is a valuable addition to existing reagents used to probe the structure and function of MHC class II molecules. This anti-HLA-DRα1 domain MAb may prove valuable for studies of HLA class II heterodimer assembly, structure, and function, as well as for studies into the release of soluble MHC class II." @default.
• W2051233616 created "2016-06-24" @default.
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• W2051233616 date "2009-12-01" @default.
• W2051233616 modified "2023-09-26" @default.
• W2051233616 title "A New Monoclonal Antibody Recognizing a Linear Determinant on the HLA-DRα Chain N-terminus" @default.
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• W2051233616 doi "https://doi.org/10.1089/hyb.2009.0050" @default.
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