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T1575

Sigma-Aldrich

Anti-Phosphotyrosine (pY-256) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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About This Item

MDL號碼:
分類程式碼代碼:
12352203
NACRES:
NA.44

生物源

rabbit

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous solution

技術

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.

儲存溫度

−20°C

目標翻譯後修改

phosphorylation (pTyr256)

一般說明

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.

免疫原

phospho-L-tyrosine containing random peptide pY-256, conjugated to KLH.

應用

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.

外觀

Solution in phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

免責聲明

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.

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儲存類別代碼

10 - Combustible liquids


分析證明 (COA)

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Wendy O White et al.
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
John Rush et al.
Nature biotechnology, 23(1), 94-101 (2004-12-14)
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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