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Anti-Phosphotyrosine Antibody, recombinant clone 4G10®, agarose conjugate

clone 4G10®, Upstate®, from mouse

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

4G10®, monoclonal

species reactivity

human

manufacturer/tradename

Upstate®

technique(s)

immunoprecipitation (IP): suitable

shipped in

wet ice

target post-translational modification

phosphorylation (pTyr)

Gene Information

human ... PID1(55022)

General description

Some of the tyrosine residues can be tagged with a phosphate group (phosphorylated) by protein kinases. (In its phosphorylated state, it is referred to as phosphotyrosine.). Tyrosine phosphorylation is considered as one of the key steps in signal transduction and regulation of enzymatic activity. The advent of anti-phospho-tyrosine antibodies is one of significant events in signal transduction research. Before the availability of anti-phosphotyrosine antibodies, tyrosyl phospyhorylation of proteins and enzymes was investigated through hazardous and time-consuming radioactive experiments. Anti-phosphotyrosine antibodies are commonly used in western blots after the targeted proteins have been immunoprecipitated to measure the tyrosyl phosphorylation of the proteins. Anti-phosphotyrosine antibodies are also directly used on cell lysate to examine the overall change of tyrosine phosphorylation level in reponse to various treatments.

Specificity

Recognizes tyrosine-phosphorylated proteins from all species.

Application

Anti-Phosphotyrosine Antibody, recombinant clone 4G10, agarose conjugate detects level of Phosphotyrosine & has been published & validated for use in IP.
Research Category
Signaling
Research Sub Category
General Post-translation Modification
This product is useful for immunoprecipitation and immunoaffinity chromatography methods.

Features and Benefits

Format: Gel Immobilized

Quality

Routinely evaluated by immunoprecipitating the EGF receptor and other tyrosine phosphorylated proteins from EGF-stimulated A431 cells.

Immunoprecipitation Analysis:
10 μL of this lot immunoprecipitated the EGF receptor and other tyrosine phosphorylated proteins from EGFstimulated A431 cells.

Target description

Dependent upon the molecular weight of the tyrosine phosphorylated protein being detected.

Physical form

Gel Immobilized mouse monoclonal antibody covalently coupled to protein A agarose beads and provided as a 50% slurry suspended in PBS, containing 0.01% Kathon, as a preservative for a total volume of 2 mL. Liquid suspension.
Protein A purified

Storage and Stability

Stable for 6 months at 2-8ºC from date of receipt.

Analysis Note

Control
Pervanadate-treated human A431 cell extracts, EGF-treated human A431 cells.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

4G10 is a registered trademark of Upstate Group, Inc.
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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.

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Xiquan Liang et al.
Journal of the American Society for Mass Spectrometry, 18(11), 1932-1944 (2007-09-18)
Protein phosphorylation regulates many aspects of cellular function, including cell proliferation, migration, and signal transduction. An efficient strategy to isolate phosphopeptides from a pool of unphosphorylated peptides is essential to global characterization using mass spectrometry. We describe an approach employing

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