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Sigma-Aldrich

Anti-acetyl Lysine Antibody, clone 4G12, agarose conjugate

clone 4G12, Upstate®, from mouse

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About This Item

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

Pricing and availability is not currently available.

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

4G12, monoclonal

species reactivity (predicted by homology)

all

manufacturer/tradename

Upstate®

technique(s)

immunoprecipitation (IP): suitable

shipped in

wet ice

target post-translational modification

acetylation (Lys)

Specificity

Recognizes acetyl lysine-containing proteins including histones.

Immunogen

A mixture of chemically acetylated antigens. Clone 4G12.

Application

Detect acetyl Lysine with Anti-acetyl Lysine Antibody, clone 4G12, agarose conjugate (Mouse Monoclonal Antibody), that has been shown to work in IP.
Research Category
Signaling

Epigenetics & Nuclear Function
Research Sub Category
General Post-translation Modification

Histones

Features and Benefits

Format: Gel Immobilized

Quality

Routinely evaluated by immunoprecipitating

Target description

varies depending upon the protein being detected

Storage and Stability

1 year at 4°C from date of shipment. DO NOT FREEZE.

Other Notes

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

Legal Information

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 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


  • Certificates of Analysis (COA)

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    Yan Liu et al.
    Journal of proteome research, 20(5), 2596-2606 (2021-04-02)
    Decreased cellular NAD+ levels are causally linked to aging and aging-associated diseases. NAD+ precursors in oxidized form such as nicotinamide mononucleotide (NMN) and nicotinamide riboside (NR) have gained much attention and been well studied for their ability to restore NAD+
    Acetylation of general transcription factors by histone acetyltransferases.
    Imhof, A, et al.
    Current Biology, 7, 689-692 (1997)
    A Villagra et al.
    Methods in enzymology, 573, 161-181 (2016-07-04)
    Histone deacetylase assays were first developed in the 1970s, and subsequently refined in the 1990s with the cloning of HDAC enzymes. Most of these early assays, relying on traditional in vitro chemical methodologies, are still applicable today. More recently, however
    N Munshi et al.
    Molecular cell, 2(4), 457-467 (1998-11-11)
    The transcriptional coactivators CBP and P/CAF are required for activation of transcription from the IFN beta enhanceosome. We show that CBP and P/CAF acetylate HMG I(Y), the essential architectural component required for enhanceosome assembly, at distinct lysine residues, causing distinct
    Fei Yue et al.
    Aging, 7(10), 839-853 (2015-11-06)
    Autophagy controls and executes the turnover of abnormally aggregated proteins. MAP1S interacts with the autophagy marker LC3 and positively regulates autophagy flux. HDAC4 associates with the aggregation-prone mutant huntingtin protein (mHTT) that causes Huntington's disease, and colocalizes with it in

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