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安全信息

B1531

Sigma-Aldrich

单克隆抗-磷酸酪氨酸

clone PT-66, purified immunoglobulin, buffered aqueous solution

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别名:
Monoclonal Anti-Phosphotyrosine, Phospho-Tyr, Phospho-tyrosine, p-Tyr
UNSPSC代码:
12352203
NACRES:
NA.44

生物来源

mouse

质量水平

偶联物

biotin conjugate

抗体形式

purified immunoglobulin

抗体产品类型

primary antibodies

克隆

PT-66, monoclonal

形式

buffered aqueous solution

技术

direct ELISA: 1:50,000
dot blot: 1:32,000

同位素/亚型

IgG1

运输

dry ice

储存温度

−20°C

靶向翻译后修饰

unmodified

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一般描述

经 ELISA 和竞争性 ELISA 确定,该抗体与磷酸化的酪氨酸特异性反应,该磷酸化的酪氨酸既可以是游离氨基酸形式,也可与 BSA 或 KLH 等载体结合的形式。与非磷酸化的酪氨酸、磷酸苏氨酸、磷酸丝氨酸、AMP 或 ATP 没有观察到交叉反应。
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.

免疫原

与 BSA 结合的磷酸酪氨酸

应用

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.

外形

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

免责声明

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.

WGK

nwg

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

含少量动物源组分生物产品
常规特殊物品

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Essential roles for Dok2 and RasGAP in CD200 receptor-mediated regulation of human myeloid cells
Mihrshahi R, et al.
Journal of Immunology, 183(8), 4879-4886 (2009)
Induction of immunoglobulin G1, interleukin-6 and interleukin-10 by Taenia crassiceps metacestode carbohydrates
Dissanayake S, et al.
Immunology, 107(4), 411-419 (2002)
A Dvir et al.
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
Wiljan J A J Hendriks et al.
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
Joanna Cieśla et al.
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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