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Merck
CN
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文件

05-813

Sigma-Aldrich

Anti-HDAC3 Antibody, clone 3G6

clone 3G6, Upstate®, from mouse

别名:

Anti-HD3

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About This Item

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

生物来源

mouse

质量水平

抗体形式

purified antibody

抗体产品类型

primary antibodies

克隆

3G6, monoclonal

种属反应性

bovine, mouse, human, hamster

制造商/商品名称

Upstate®

技术

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

同位素/亚型

IgG2a

NCBI登记号

UniProt登记号

运输

wet ice

靶向翻译后修饰

unmodified

基因信息

human ... HDAC3(8841)

一般描述

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.

特异性

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

免疫原

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

应用

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

质量

routinely evaluated by immunoprecipitation/HDAC

目标描述

49-53kDa

外形

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

储存及稳定性

2 years at -20°C

分析说明

Control
HL-60 cell lysate

法律信息

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

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.

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WGK

WGK 1


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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
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
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
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
Thomas W Hanigan et al.
PloS one, 12(10), e0186620-e0186620 (2017-10-19)
The mechanism of action of histone deacetylase inhibitors (HDACi) is mainly attributed to the inhibition of the deacetylase catalytic activity for their histone substrates. In this study, we analyzed the abundance of class I HDACs in the cytosolic, nuclear soluble

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