Abstract
An antiserum was generated against a C-terminal peptide of the mouse activin type II receptor (ActR-II), which specifically immunoprecipitates ActR-II protein transiently expressed in COS-1 cells. Autophosphorylation activity of the ActR-II was examined in [32P]orthophosphate labeled COS-1 cells. The immunoprecipitated ActR-II protein was found to be phosphorylated on serine residues in the absence of ligand stimulation, and the phosphorylation was slightly increased after stimulation with activin A.
MeSH terms
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Activin Receptors
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Activins
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Amino Acid Sequence
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Animals
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Cells, Cultured
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Inhibins / metabolism*
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Mice
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Molecular Sequence Data
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Peptide Fragments / immunology
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Phosphorylation
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Protein Serine-Threonine Kinases / immunology
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Protein Serine-Threonine Kinases / metabolism*
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Receptors, Cell Surface / immunology
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Receptors, Cell Surface / metabolism*
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Substrate Specificity
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Transfection
Substances
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Peptide Fragments
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Receptors, Cell Surface
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Activins
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Inhibins
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Protein Serine-Threonine Kinases
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Activin Receptors