Monoclonal antibody B9-2 recognizes an 8 amino acid sequence that spans an autocatalytic cleavage site between the two subunits of human procaspase 8.
Caspase 8 is synthesized in a zymogen form and must be proteolytically cleaved to be activated. The catalytically active enzyme is composed of two of the four cleavage products. We have determined that the monoclonal antibody B9-2 recognizes the octomer EMDLSSPQ. This sequence is shared by two of the cleavage products: a decamer linker region released after autocatalysis and the smaller subunit of the active enzyme.
Ellis
B
B
Department of Molecular Sciences, Glaxo Wellcome Research and Development, Research Triangle Park, NC 27709, USA.
Weaver
K
K
Dallas
W S
WS
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology*; D015374:Biosensing Techniques; D053181:Caspase 8; D053453:Caspase 9; D020169:Caspases / Q000737:chemistry / Q000276:immunology*; D004789:Enzyme Activation / Q000276:immunology; D004792:Enzyme Precursors / Q000737:chemistry / Q000276:immunology*; D018604:Epitope Mapping; D006801:Humans; D009842:Oligopeptides / Q000276:immunology; D010446:Peptide Fragments / Q000276:immunology; D017434:Protein Structure, Tertiary
D000911:Antibodies, Monoclonal; D004792:Enzyme Precursors; D009842:Oligopeptides; D010446:Peptide Fragments; C505530:CASP8 protein, human; C506433:CASP9 protein, human; D053181:Caspase 8; D053453:Caspase 9; D020169:Caspases