Two widely used anti-DR alpha monoclonal antibodies bind to an intracellular C-terminal epitope.
In this report we show that two widely-used monoclonal antibodies, TAL-1B5 and DA6.147, which react with the HLA-DR alpha chain on immunoblots, recognize the C-terminal intracellular tail of this HLA-DR subunit. We demonstrate that both MoAbs react with a synthetic peptide representing the intracellular C-terminal tail of the DR alpha chain and that mutant DR molecules lacking this part of the alpha chain lose reactivity with TAL-1B5 and DA6.147, both in Western blot analysis and in intracellular FACS staining.
Grüneberg
U
U
Human Immunogenetics Group, Imperial Cancer Research Fund, London, United Kingdom.
Rich
T
T
Roucard
C
C
Marieke van Ham
S
S
Charron
D
D
Trowsdale
J
J
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000378:metabolism*; D001666:Binding Sites, Antibody; D000939:Epitopes / Q000276:immunology* / Q000378:metabolism*; D006684:HLA-DR Antigens / Q000235:genetics / Q000276:immunology* / Q000378:metabolism*; D006801:Humans; D007424:Intracellular Fluid / Q000276:immunology; D008969:Molecular Sequence Data; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D000939:Epitopes; D006684:HLA-DR Antigens