B1531
Monoclonal Anti-Phosphotyrosine−Biotin antibody produced in mouse
clone PT-66, purified immunoglobulin, buffered aqueous solution
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Monoclonal Anti-Phosphotyrosine, Phospho-Tyr, Phospho-tyrosine, p-Tyr
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biological source
mouse
Quality Level
conjugate
biotin conjugate
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
PT-66, monoclonal
form
buffered aqueous solution
technique(s)
direct ELISA: 1:50,000
dot blot: 1:32,000
isotype
IgG1
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
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General description
As determined by ELISA and competitive ELISA, the antibody reacts specifically with phosphorylated tyrosine, both as free amino acid or conjugated to carriers such as BSA or KLH. No cross-reactivity is observed with non-phosphorylated tyrosine, phosphothreonine, phosphoserine, AMP or ATP.
Monoclonal Anti-Phosphotyrosine (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.
Reversible phosphorylation of proteins is an important post-translational modification that plays a regulatory role in the expression of most proteins in the cells. Reversible phosphorylation at multiple serine, tyrosine and threonine residues mediates numerous signalling pathways in both prokaryotic and eukaryotic cells . Cellular proteins with phosphorylated tyrosine increase many fold by the activation of tyrosine kinases. Most mitogenic receptor systems such as EGF, PDGF, insulin receptors contain serine/threonine/tyrosine kinase domains that undergo autophosphorylation when receptors bind to the respective ligands. Monoclonal anti-phosphotyrosine?biotin antibody can be used in dot blot (diluted 1:32,000). Mouse anti-phosphotyrosine?biotin antibody reacts specifically with phosphorylated tyrosine both as the free amino acid or when conjugated to BSA or KLH. This product does not react with non-phosphorylated tyrosine or other phosphorylated amino acids, including serine and threonine, or with phosphorylated molecules like AMP or ATP.
Immunogen
phosphotyrosine conjugated to BSA
Application
Monoclonal Anti-Phosphotyrosine?Biotin antibody produced in mouse has been used in western blot analysis to detect tyrosine phosphorylated proteins. It has also been used in BIAcore analysis. This conjugate maybe used as an analytical tool by enabling the identification and quantification of tyrosine phosphorylated proteins.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
含少量动物源组分生物产品
常规特殊物品
Certificates of Analysis (COA)
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Essential roles for Dok2 and RasGAP in CD200 receptor-mediated regulation of human myeloid cells
Journal of Immunology, 183(8), 4879-4886 (2009)
Induction of immunoglobulin G1, interleukin-6 and interleukin-10 by Taenia crassiceps metacestode carbohydrates
Immunology, 107(4), 411-419 (2002)
The Journal of cell biology, 113(4), 857-865 (1991-05-01)
Protein tyrosine kinase blockers of the tyrphostin family inhibited the EGF-dependent proliferation of human and guinea pig keratinocytes grown in culture and induced their growth arrest. These blockers also significantly inhibited the growth of epidermal keratinocytes, but not of dermal
The FEBS journal, 275(5), 816-830 (2008-02-27)
Some 40-odd genes in mammals encode phosphotyrosine-specific, 'classical' protein tyrosine phosphatases. The generation of animal model systems and the study of various human disease states have begun to elucidate the important and diverse roles of protein tyrosine phosphatases in cellular
Acta biochimica Polonica, 58(2), 137-148 (2011-05-31)
Reversible phosphorylation is the most widespread posttranslational protein modification, playing regulatory role in almost every aspect of cell life. The majority of protein phosphorylation research has been focused on serine, threonine and tyrosine that form acid-stable phosphomonoesters. However, protein histidine
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