Premium
Characterization of a Monoclonal Antibody Directed Against the Phosphotyrosine Kinase p56 lck , in Human T Cells
Author(s) -
ANSOTEGUI I. J.,
CHOW S. C.,
JEDDITEHRANI M.,
MELOCHE S.,
PAWSON A.,
SEKALY R.P.,
MAKI T. W.,
WIGZELL H.
Publication year - 1991
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1991.tb01784.x
Subject(s) - monoclonal antibody , tyrosine kinase , microbiology and biotechnology , kinase , antibody , transmembrane protein , chemistry , signal transduction , biology , receptor , biochemistry , immunology
A monoclonal antibody (anti‐p56 lck ) was generated against a fusion protein containing the residues 145–509 of the human p56 lck , a lymphoeyte‐specific membrane‐associated protein tyrosine kinase. The involvement of this enzyme in T‐cell transmembrane signalling seems to be an early and crucial event during T‐cell receptor‐mediated activation. We have produced a monoclonal antibody which recognizes p56 lck in free form and when associated with CD4. H functions in western blot analysis and is capable of selectively blocking auto‐phosphorylation of this kinase. This monoclonal antibody should be useful for investigating the role of p56 lck in T‐cell activation.