Detects proteins containing phosphorylated tyrosine residues. ELISA and 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. No cross‑reactivity with proteins or peptides containing phosphorylated serine or threonine residues is observed.
Monoclonal Mouse IgG1 Clone # 179003
Protein A or G purified from hybridoma culture supernatant
KLH-coupled phospho-tyrosine synthetic peptide
Supplied in a saline solution containing BSA and Sodium Azide.
Intracellular Staining by Flow Cytometry
10 µL/106 cells
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 in Human PBMCs by Flow Cytometry. Human peripheral blood mononuclear cell (PBMCs) either (A) untreated or (B) treated with PMA were stained with Mouse Anti-Phospho-Tyrosine PE‑conjugated Monoclonal Antibody (Catalog # IC1676P). Quadrant markers were set based upon isotype control staining (Catalog # IC002P; data not shown). View our protocol for Staining Intracellular Molecules.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Tyrosine phosphorylation is considered to be one of the key steps in signal transduction and regulation of enzymatic activity. The phosphorylation of specific tyrosine residues has been shown to be a primary mechanism of signal transduction during normal cell cycle progression and oncogenic transformation. The role of tyrosine phosphorylation is a matter of active and ongoing research. Specific antibodies that recognize phosphorylated tyrosine residues are valuable to the study of tyrosine phosphorylated proteins and the biochemical pathways in which they are involved.