|Related Categories||Alphabetical Index, Antibodies, Antibodies for Cell Biology, Antibodies for Kinase/Phosphatase Biology, Antibodies to Phosphoproteins,|
|antibody form||purified immunoglobulin|
|form||buffered aqueous glycerol solution|
|western blot: suitable|
|shipped in||wet ice|
Solution in 20 mM phosphate buffered saline, pH 7.5, containing 50% glycerol and 3 mM sodium azide
Immunohistochemistry was performed on formalin-fixed paraffin-embedded mouse brain sections (4 microns) using mouse monoclonal anti-phosphotyrosine antibody at 1:1500. To enhance the signal, sections were treated with formic acid for 5 minutes and then microwaved at 90 degrees for 1 hour before incubation with the antibody. 1
Immunohistochemistry was performed on formalin-fixed paraffin-embedded mouse brain sections (4 microns) using mouse monoclonal anti-phosphotyrosine antibody at 1:1500. To enhance the signal, sections were treated with formic acid for 5 minutes and then microwaved at 90 degrees for 1 hour before incubation with the antibody.1
Mouse monoclonal clone PY20 anti-Phosphotyrosine is specific for both native and denatured proteins containing phosphorylated tyrosine. Antibody binding is inhibited with phosphotyrosine and phenylphosphate, but not phosphoeserine or phosphothreonine.
Protein phosphorylation is a basic mechanism for the modification of protein function in eukaryotic cells. Tyrosine phosphorylation is a rare post-translational event in normal tissue, accounting for only 0.03% of phosphorylated amino acids. The level of phosphorylated tyrosine in many cellular proteins increases tenfold following various activation processes that are mediated through phosphotyrosine kinases. The importance of tyrosine phosphorylation has been established by the demonstration that it is an integral response in many different mitogenic receptor systems.
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 mediate 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 tyrosine kinase domains that undergo autophosphorylation when receptors bind to the respective ligands. Tyrosine-specific protein kinase activity has also been described in many retroviral oncogene proteins. Cells transformed by these oncogenes contain elevated levels of phosphotyrosine. Many of the oncogenes found in mammalian oncogenic viruses encode tyrosine protein kinases that reside in the cellular cytoplasm. Others encode transmembrane receptors whose tyrosine phosphotransferase activity is stimulated by the binding of ligand to the extracellular domain.
Monoclonal Anti-Phosphotyrosine is specific for both native and denatured proteins containing phosphorylated tyrosine.
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Keywords: Buffers, Cell biology, Epigenetics, Immunohistochemistry, Immunoprecipitation, Molecular biology, Neuroscience, Western blot
Distinct modes of activation of phosphatidylinositol 3-kinase in response to cyclic adenosine 3′,5′-monophosphate or insulin-like growth factor I play different roles in regulation of cyclin D1 and p27Kip1 in FRTL-5 cells. Akahori, M., et al. Endocrinology 149, 3729-3742, (2008)
The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and the recruitment of both pp125FAK and protein kinase C-delta to focal adhesions. Barry, S.T., and Critchley, D.R. J. Cell Sci. 107, 2033-2045, (1994)
Heavy and light chain variable region sequences and antibody properties of anti-phosphotyrosine antibodies reveal both common and distinct features. Ruff-Jamison, AS., et al. J. Biol. Chem. 266, 6607, (1991)
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