Mouse polyclonal Tob antibody Background: A cDNA for a novel protein termed Tob (Transducer of ErbB2) that interacts with the cerbB2 gene product p185erbB2 was molecularly cloned. Nucleotide sequencing reveals that the Tob protein is a 45 kDa protein that does not contain either SH2 or SH3 domain but is homologous to the previously characterized antiproliferative gene product BTG1 at its amino terminal half. The carboxyl terminal half of Tob is characterized by the presence of a sequence rich in proline and glutamine and shows no homology to known proteins. Like BTG1, exogenously expressed Tob is able to suppress growth of NIH3T3 cells, but the growth suppression is hampered by the presence of kinase active p185erbB2. By using the SGTTob protein that contains either full length or amino terminal half of Tob, The carboxyl terminal half of Tob is relevant to its interaction with p185erbB2. In addition, coimmunoprecipitatio
n of the Tob protein with antiErbB2 antibody and reciprocally the p185erbB2 with antiTob antibodies could be conducted. These data suggest that p185erbB2 negatively regulates the Tob-mediated antiproliferative pathway through its interaction with Tob. The expression of the Tob mRNA is observed in various cell types and is not correlated with expression of cerbB2, suggesting that other receptor-type protein tyrosine kinases are also involved the Tob-mediated regulation of cell growth.
Mouse polyclonal Tob antibody
Background:
A cDNA for a novel protein termed Tob (Transducer of ErbB2) that interacts with the cerbB2 gene product p185erbB2 was molecularly cloned. Nucleotide sequencing reveals that the Tob protein is a 45 kDa protein that does not contain either SH2 or SH3 domain but is homologous to the previously characterized antiproliferative gene product BTG1 at its amino terminal half. The carboxyl terminal half of Tob is characterized by the presence of a sequence rich in proline and glutamine and shows no homology to known proteins. Like BTG1, exogenously expressed Tob is able to suppress growth of NIH3T3 cells, but the growth suppression is hampered by the presence of kinase active p185erbB2. By using the SGTTob protein that contains either full length or amino terminal half of Tob, The carboxyl terminal half of Tob is relevant to its interaction with p185erbB2. In addition, coimmunoprecipitation of the Tob protein with antiErbB2 antibody and reciprocally the p185erbB2 with antiTob antibodies could be conducted. These data suggest that p185erbB2 negatively regulates the Tob-mediated antiproliferative pathway through its interaction with Tob. The expression of the Tob mRNA is observed in various cell types and is not correlated with expression of cerbB2, suggesting that other receptor-type protein tyrosine kinases are also involved the Tob-mediated regulation of cell growth.
