Detects proteins containing phosphorylated tyrosine residues. ELISA and 2D Western blot analyses using pervanadate-treated cell lysates indicate that clone 179003 binds Phospho-Tyrosine in a broad manner largely independent of the surrounding amino acid sequence. The antibody does not cross-react with proteins or peptides containing phosphorylated serine or threonine residues.
Monoclonal Mouse IgG1 Clone # 179003
Protein A or G purified from hybridoma culture supernatant
KLH-coupled Phospho-Tyrosine synthetic peptide
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
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 µg/mL of Mouse Anti-Phospho-Tyrosine Biotinylated Monoclonal Antibody (Catalog # BAM1676), followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). Tyrosine-phosphorylated proteins were detected (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 10.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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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