Development and Characterization of Monoclonal Antibodies to Bovine Brain Calcineurin

1 February 1987

journal article
research article
Published by Mary Ann Liebert Inc in Hybridoma

Vol. 6 (1) , 77-85
https://doi.org/10.1089/hyb.1987.6.77

Abstract

Three monoclonal antibodies (MAb's) against bovine brain calcineurin, a Ca⁺⁺-calmodulin dependent phosphatase, have been developed and characterized. Among these antibodies, two are α-subunit (60,000 Mr) specific and one is β-subunit (19,000 Mr) specific. These antibodies also cross-react with similar proteins obtained from brains of human, rat and mouse. The methodology for raising these antibodies and their properties are described.

Keywords

This publication has 16 references indexed in Scilit:

Characterization of phosphotyrosyl-protein phosphatase activity associated with calcineurin
Biochemical and Biophysical Research Communications, 1984
Activation of calcineurin by limited proteolysis.
Proceedings of the National Academy of Sciences, 1983
[20] Use of calmodulin affinity chromatography for purification of specific calmodulin-dependent enzymes
Published by Elsevier ,1983
One-step purification of mouse monoclonal antibodies from ascitic fluid by DEAE Affi-gel blue chromatography
Journal of Immunological Methods, 1982
Calcineurin is a calmodulin-dependent protein phosphatase
Biochemical and Biophysical Research Communications, 1982
Discovery of A Ca²⁺‐and calmodulin‐dependent protein phosphatase
FEBS Letters, 1982
High levels of a heat-labile calmodulin-binding protein (CaM-BP80) in bovine neostriatum
Biochemistry, 1980
Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
Proceedings of the National Academy of Sciences, 1979
Purification of cyclic 3',5'-nucleotide phosphodiesterase inhibitory protein by affinity chromatography on activator protein coupled to sepharose
Biochemistry, 1978
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Nature, 1970