Non-Neutralizing Monoclonal Antibodies Against RAS GTPase-Activating Protein: Production, Characterization and Use in an Enzyme Immunometric Assay

We studied several monoclonal antibodies (mAbs) raised against the 100 kD Ras GTPase activating protein (p100–GAP), which was purified from human placenta. These antibodies recognized p120–GAP and p100–GAP in native and in denatured forms. The most reactive, GP15 and GP200, both recognized distinct...

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Bibliographic Details
Published in:Bio/Technology 1992-10, Vol.10 (10), p.1151-1156
Main Authors: Mollat, P, Zhang, G. Y, Frobert, Y, Zhang, Y. H, Fournier, A, Grassi, J, Thang, M. N
Format: Article
Language:English
Subjects:
Agriculture
Animals
Antibodies, Monoclonal - isolation & purification
Bioinformatics
Biomedical and Life Sciences
Biomedical Engineering/Biotechnology
Biomedicine
Biotechnology
Cell Line
Choriocarcinoma - chemistry
Genes, ras
GTPase-Activating Proteins
Humans
Immunoenzyme Techniques
Life Sciences
Mice
Placental Extracts - chemistry
Proteins - analysis
Proteins - isolation & purification
Proteins - metabolism
ras GTPase-Activating Proteins
research-paper
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Summary:We studied several monoclonal antibodies (mAbs) raised against the 100 kD Ras GTPase activating protein (p100–GAP), which was purified from human placenta. These antibodies recognized p120–GAP and p100–GAP in native and in denatured forms. The most reactive, GP15 and GP200, both recognized distinct epitopes and did not neutralize GTPase stimulatory activity. These two mAbs were selected for a two–site enzyme immunoassay, using covalent conjugates of the antibodies coupled to the tetrameric form of acetylcholinesterase as tracer. This assay was used to quantify Ras–GAP in both normal and tumor tissues and cell extracts.
ISSN:0733-222X
1087-0156
2331-3684
1546-1696
DOI:10.1038/nbt1092-1151