Detects 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. This antibody 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
Please refer to the PDF datasheet for specifications.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Phospho-Tyrosine by Western Blot. Western blot shows lysates of A431 human epithelial carcinoma cell line untreated (-) or treated (+) with 50 μM pervanadate (PV) for 15 minutes. PVDF membrane was probed with 1:1000 dilution of Phospho-Tyrosine AP-conjugated Monoclonal Antibody (Catalog # APM1676), followed by [Secondary Antibody Proper Name & Link]. Tyrosine-phosphorylated proteins were detected (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group XXX.
Preparation and Storage
Sterile PBS to a final concentration of 0.5 mg/mL.
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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