indirect immunofluorescence: 5-10 μg/mL using A431 stimulated by human EGF. western blot: 0.5-1.0 μg/mL using cell extract of A431 stimulated by human EGF.
storage temp.
−20°C
target post-translational modification
phosphorylation (pTyr256)
General description
Protein phosphorylation is a post-translational modification that regulates signal transduction. Phosphorylation of tyrosine residues in proteins has been associated with oncogenesis, cell growth and survival . Phosphotyrosines have also been linked to other cellular functions. For instance, tyrosine 256 phosphorylation in atypical protein kinase C enables its entry into the nucleus of cells . Anti-Phosphotyrosine pTyr256 binds to tyrosine phosphorylated proteins. In immunoblotting, the antibody detects [pTyr256] in random peptides and phospho-L-tyrosine, but does not react with phospho-L-serine, phospho-L-threonine and L-tyrosine.
Immunogen
phospho-L-tyrosine containing random peptide pY-256, conjugated to KLH.
Application
Anti-Phosphotyrosine (pY-256) antibody is suitable for use in western blot (1:1000) . It may also be used in indirect immunofluorescence (5-10 μg/mL using A431 stiμLated by human EGF), immunoblotting and immunocytochemistry.
Physical form
Solution in phosphate buffered saline, pH 7.4, containing 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.
Journal of cellular biochemistry, 85(1), 42-53 (2002-03-14)
Herein, we employed a combined approach of molecular modeling and site-directed mutagenesis to address the role of tyrosine phosphorylation in transport of atypical protein kinase C (aPKC) into the nucleus. Computer modeling of the three-dimensional structure of the aPKC catalytic
Tyrosine kinases play a prominent role in human cancer, yet the oncogenic signaling pathways driving cell proliferation and survival have been difficult to identify, in part because of the complexity of the pathways and in part because of low cellular
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