Detects endogenous proteins containing phosphorylated tyrosine residues. ELISA and 2D Western blot analyses using pervanadate-treated cell lysates indicate that it binds Phospho-Tyrosine in a broad manner largely independent of the surrounding amino acid sequence. Does not cross-react with proteins or peptides containing phosphorylated serine or threonine residues.
Monoclonal Mouse IgG1 Clone # 179003
Supplied as a 0.2 μm filtered solution in phosphate-buffered saline (PBS) with stabilizers
Sterile PBS to a final concentration of 0.5 mg/mL.
Reconstitution Buffer Available
Stability & Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
Phosphorylation of tyrosine residues in signaling proteins by protein tyrosine kinases mediates a variety of cellular processes, including cell growth, differentiation, adhesion, motility, death, and metabolism. Dysregulation of tyrosine phosphorylation has been implicated in the development of many human diseases, such as diabetes and cancer. Antibodies specific for phospho-tyrosine have been invaluable reagents in the studies of signaling pathways initiated by tyrosine phosphorylation.
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