Production and evaluation of a monoclonal antibody against human myeloperoxidase
In Indian Journal of Medical Research
By: Badrinath Y.
Contributor(s): Advani SH | Narkar AA | Nair CN | Bajpai S | Dhond SR | .
Material type:
ArticleSeries: Vol 105 Issues.Publisher: 1997Description: 176-179.Subject(s): LeukemiaDDC classification: 616.155
In:
Indian Journal of Medical ResearchSummary: We describe the production of a mouse monoclonal antibody (H2E1) against human myeloperoxidase antigen. After production and characterisation, this antibody was compared with commercially available monoclonal antibodies, cytochemical myeloperoxidase and previously produced polyclonal antibody. Reaction with various cell lines proved that this monoclonal antibody was specific for myeloid lineage. This monoclonal showed positivity in 81.8 per cent of acute myeloid leukaemias whereas the polyclonal antibody was 100 per cent positive. We found that the polyclonal antibody was more sensitive as compared to the monoclonal. This is probably due to the lack of recognition of individual epitopes on the antigen. We recommend the use of antibodies which have different epitope recognition as most specific for myeloperoxidase
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Tata Memorial Hospital | 616.155 | Available | AR1271 |
We describe the production of a mouse monoclonal antibody (H2E1) against human myeloperoxidase antigen. After production and characterisation, this antibody was compared with commercially available monoclonal antibodies, cytochemical myeloperoxidase and previously produced polyclonal antibody. Reaction with various cell lines proved that this monoclonal antibody was specific for myeloid lineage. This monoclonal showed positivity in 81.8 per cent of acute myeloid leukaemias whereas the polyclonal antibody was 100 per cent positive. We found that the polyclonal antibody was more sensitive as compared to the monoclonal. This is probably due to the lack of recognition of individual epitopes on the antigen. We recommend the use of antibodies which have different epitope recognition as most specific for myeloperoxidase
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