Reversible phosphorylation of proteins is an important post-translational modification that plays a regulatory role in the expression of most proteins in the cells. Reversible phosphorylation at multiple serine, tyrosine and threonine residues mediates numerous signalling pathways in both prokaryotic and eukaryotic cells . Cellular proteins with phosphorylated tyrosine increase many fold by the activation of tyrosine kinases. Most mitogenic receptor systems such as EGF, PDGF, insulin receptors contain serine/threonine/tyrosine kinase domains that undergo autophosphorylation when receptors bind to the respective ligands. Monoclonal anti-phosphotyrosine−agarose antibody can be used in immunoprecipitation. Mouse anti-phosphotyrosine−agarose antibody reacts specifically with both native and denatured proteins comprising phosphorylated tyrosine.
Immunogen
phosphotyrosine-protein conjugate
Application
Monoclonal anti-phosphotyrosine−agarose antibody can be used in immunoaffinity purification of phosphotyrosyl proteins, including transforming proteins, steroid hormone receptors (e.g., estradiol and glucocorticoid receptors), growth factor receptors (e.g., EGF and PDGF receptors), insulin receptors and other proteins involved in the control of cellular growth.
Physical form
Suspension in 20 mM sodium phosphate, pH 7.5, 150 mM sodium chloride, 3 mM sodium azide.
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CEACAM1 expressed by granulocytes and epithelial cells is recognized as a membrane-associated receptor by some Gram-negative pathogens. Here we report a previously unsuspected role of human CEACAM1-4L (hCEACAM1-4L) in polarized epithelial cells. We find that in contrast with non-transfected cells
The Journal of cell biology, 113(4), 857-865 (1991-05-01)
Protein tyrosine kinase blockers of the tyrphostin family inhibited the EGF-dependent proliferation of human and guinea pig keratinocytes grown in culture and induced their growth arrest. These blockers also significantly inhibited the growth of epidermal keratinocytes, but not of dermal
Some 40-odd genes in mammals encode phosphotyrosine-specific, 'classical' protein tyrosine phosphatases. The generation of animal model systems and the study of various human disease states have begun to elucidate the important and diverse roles of protein tyrosine phosphatases in cellular
Reversible phosphorylation is the most widespread posttranslational protein modification, playing regulatory role in almost every aspect of cell life. The majority of protein phosphorylation research has been focused on serine, threonine and tyrosine that form acid-stable phosphomonoesters. However, protein histidine
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