Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-12-12
pubmed:abstractText
Six hybridomas secreting monoclonal antibodies that are specific for the N-terminal peptide sequence of the murine Ah receptor were isolated. These antibodies bind with high specificity to the Ah receptor on protein blots of Hepa 1c1c7 cytosol. Three IgG1 antibodies (Rpt 1, 2, and 3) were capable of detecting 2 ng of receptor using peroxidase-goat anti-mouse IgG antibody conjugate on a protein blot. Monoclonal antibody Rpt 9 exhibited the greatest ability to immunoprecipitate the nondenatured 9S form of the Ah receptor and to visualize the AhR on liver tissue sections using immunohistochemical techniques. All of the monoclonal antibodies produced were able to bind to the mouse, rat, and human Ah receptor. These monoclonal antibodies should be useful in a wide number of applications in the study of Ah receptor biochemistry.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0272-457X
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
279-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Production and characterization of monoclonal antibodies directed against the Ah receptor.
pubmed:affiliation
Department of Foods and Nutrition, Purdue University, West Lafayette, Indiana 47907, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.