Monoclonal antibody B9-2 recognizes an 8 amino acid sequence that spans an autocatalytic cleavage site between the two subunits of human procaspase 8

B Ellis; K Weaver; W S Dallas

doi:10.1089/02724570050031211

Monoclonal antibody B9-2 recognizes an 8 amino acid sequence that spans an autocatalytic cleavage site between the two subunits of human procaspase 8

Hybridoma. 2000 Apr;19(2):167-9. doi: 10.1089/02724570050031211.

Authors

B Ellis¹, K Weaver, W S Dallas

Affiliation

¹ Department of Molecular Sciences, Glaxo Wellcome Research and Development, Research Triangle Park, NC 27709, USA.

PMID: 10868797
DOI: 10.1089/02724570050031211

Abstract

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.

MeSH terms

Amino Acid Sequence
Antibodies, Monoclonal / immunology*
Biosensing Techniques
Caspase 8
Caspase 9
Caspases / chemistry
Caspases / immunology*
Enzyme Activation / immunology
Enzyme Precursors / chemistry
Enzyme Precursors / immunology*
Epitope Mapping
Humans
Oligopeptides / immunology
Peptide Fragments / immunology
Protein Structure, Tertiary

Substances

Antibodies, Monoclonal
Enzyme Precursors
Oligopeptides
Peptide Fragments
CASP8 protein, human
CASP9 protein, human
Caspase 8
Caspase 9
Caspases