Phosphotyrosine antibody

Details for Product No. ABIN361806
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Antigen
Reactivity
(150), (62), (47), (32), (29), (24), (13), (8), (8), (3), (1)
Host
Mouse
(217), (62), (2)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(30), (26), (22), (17), (9), (4), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1)
Application
ELISA, Western Blotting (WB)
(206), (125), (101), (74), (70), (52), (33), (32), (15), (12), (10), (2), (2), (1), (1), (1), (1)
Pubmed 7 references available
Quantity 100 μL
Options
Shipping to United States ( )
Availability Please contact our customer support.
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Immunogen Phosphotyrosine conjugated to KLH
Clone 13F9
Isotype IgG1 kappa
Specificity Reacts with phosphotyrosine, and detects the presence of phosphotyrosine in both un-stimulated and stimulated cell lysates. Does not cross-react with phosphoserine or phosphothreonine.
Cross-Reactivity (Details) Does not cross-react with phosphoserine or phosphothreonine.
Purification Ascites
Background Protein phosphorylation is an important posttranslational modification that serves many key functions to regulate a protein’s activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various specific protein kinases, which involves removing a phosphate group from ATP and covalently attaching it to to a recipient protein that acts as a substrate. Most kinases act on both serine and threonine, others act on tyrosine, and a number (dual specificity kinases) act on all three. Because phosphorylation can occur at multiple sites on any given protein, it can therefore change the function or localization of that protein at any time. Changing the function of these proteins has been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders.In particular, the phosphorylation of tyrosine is considered one of the key steps in signal transduction and regulation of enzymatic activity. Phosphotyrosine can be detected through specific antibodies, and are helpful in facilitating the identification of tyrosine kinase substrates.
Research Area Signaling, Metabolism, Amino Acids, Protein Modifications, Cell Signaling
Application Notes Recommended Dilution: 1:2000 to 1:10000
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Storage -20 °C
Background publications Goto, Kiyono, Tomono et al.: "Complex formation of Plk1 and INCENP required for metaphase-anaphase transition." in: Nature cell biology, Vol. 8, Issue 2, pp. 180-7, 2006 (PubMed).

Downward: "The ins and outs of signalling." in: Nature, Vol. 411, Issue 6839, pp. 759-62, 2001 (PubMed).

Blume-Jensen, Hunter: "Oncogenic kinase signalling." in: Nature, Vol. 411, Issue 6835, pp. 355-65, 2001 (PubMed).

Pawson, Saxton: "Signaling networks--do all roads lead to the same genes?" in: Cell, Vol. 97, Issue 6, pp. 675-8, 1999 (PubMed).

Ostrovsky, Maloy: "Protein phosphorylation on serine, threonine, and tyrosine residues modulates membrane-protein interactions and transcriptional regulation in Salmonella typhimurium." in: Genes & development, Vol. 9, Issue 16, pp. 2034-41, 1995 (PubMed).

Ross, Baltimore, Eisen: "Phosphotyrosine-containing proteins isolated by affinity chromatography with antibodies to a synthetic hapten." in: Nature, Vol. 294, Issue 5842, pp. 654-6, 1982 (PubMed).

General Frackelton, Ross, Eisen: "Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells." in: Molecular and cellular biology, Vol. 3, Issue 8, pp. 1343-52, 1983 (PubMed).

Validation Images
Catalog No. ABIN361806
349.80 $
Plus shipping costs $45.00
Add to Basket

Order hotline:

  • +1 877 302 8632
  • +1 888 205 9894 (TF)
Did you look for something else?