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Key Documents

05-813

Sigma-Aldrich

Anti-HDAC3 Antibody, clone 3G6

clone 3G6, Upstate®, from mouse

Sinónimos:

Anti-HD3

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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

3G6, monoclonal

species reactivity

bovine, mouse, human, hamster

manufacturer/tradename

Upstate®

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2a

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... HDAC3(8841)

General description

Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. HDAC3 belongs to the histone deacetylase/acuc/apha family. It has histone deacetylase activity and represses transcription when tethered to a promoter. It may participate in the regulation of transcription through its binding with the zinc-finger transcription factor YY1. This protein can also down-regulate p53 function and thus modulate cell growth and apoptosis. HDAC3 is regarded as a potential tumor suppressor gene.

Specificity

HDAC3
Predicted to cross-react with rat and chicken based on sequence homology

Immunogen

peptide (NEFYDGDHDNDKESDVEI) corresponding to amino acids 411-428 of human HDAC3

Application

Anti-HDAC3 Antibody, clone 3G6 is a Mouse Monoclonal Antibody for detection of HDAC3 also known as histone deacetylase 3 & has been tested in IP, WB, ICC.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Histones

Quality

routinely evaluated by immunoprecipitation/HDAC

Target description

49-53kDa

Physical form

0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol to 30%.
Format: Purified
Protein G Purified

Storage and Stability

2 years at -20°C

Analysis Note

Control
HL-60 cell lysate

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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Referencia del producto
Descripción
Precios

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1


Certificados de análisis (COA)

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Chun Guo et al.
The Journal of biological chemistry, 295(13), 4212-4223 (2020-02-20)
In up to 15% of acute myeloid leukemias (AMLs), a recurring chromosomal translocation, termed t(8;21), generates the AML1-eight-twenty-one (ETO) leukemia fusion protein, which contains the DNA-binding domain of Runt-related transcription factor 1 (RUNX1) and almost all of ETO. RUNX1 and
Hong-Ling Zhao et al.
Biochemical and biophysical research communications, 383(1), 119-124 (2009-04-04)
Recent data has implicated the Ski protein as being a physiologically relevant negative regulator of signaling by retinoic acid (RA). The mechanism by which Ski represses RA signaling is unknown. Co-immunoprecipitation and immunofluorescence assay showed that Ski and RARalpha are
Wolfgang Fischle et al.
Molecular cell, 9(1), 45-57 (2002-01-24)
Histone deacetylases (HDACs) play a key role in regulating eukaryotic gene expression. The HDAC domain, homologous to the yeast repressors RPD3 and HDA1, is considered necessary and sufficient for enzymatic activity. Here, we show that the catalytic domain of HDAC4
Histone deacetylases: unique players in shaping the epigenetic histone code.
Thiagalingam, Sam, et al.
Annals of the New York Academy of Sciences, 983, 84-100 (2003)
Michael Nevels et al.
Proceedings of the National Academy of Sciences of the United States of America, 101(49), 17234-17239 (2004-12-02)
The human cytomegalovirus 72-kDa immediate-early (IE)1 and 86-kDa IE2 proteins are expressed at the start of infection, and they are believed to exert much of their function through promiscuous transcriptional activation of viral and cellular gene expression. Here, we show

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