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Merck
CN
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文件

07-937

Sigma-Aldrich

Anti-HDAC7 Antibody

from rabbit, purified by affinity chromatography

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别名:
histone deacetylase 7, histone deacetylase 7A
UNSPSC代码:
12352203
eCl@ss:
32160702
NACRES:
NA.41

生物来源

rabbit

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

纯化方式

affinity chromatography

种属反应性

human

技术

western blot: suitable

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 ... HDAC7(51564)

一般描述

Histone deacetylases (HDAC) are enzymes that regulates transcription by selectively deacetylating the eta-amino groups of lysines located near the amino termini of core histone proteins. Eight members of the HDAC family have been identified, divided in to two classes. Class I includes HDAC-1, 2, 3 and 8 while Class II includes HDAC-4, 5, 6, and 7. Human HDAC7 is composed of 912 amino acid residues. Although HDAC7 is localized mostly to the cell nucleus, it is also found in the cytoplasm, suggesting nucleo-cytoplasmic shuttling. The histone deacetylase activity of HDAC7 maps to a C-terminal domain and is dependent on interaction with class I HDACs in the nucleus. It is an active component of different transcriptional co-repressor complexes that can be recruited to specific promoter regions via interactions with transcription factors. HDAC7 catalyzes removal of acetyl-groups from acetyl-lysines of histones, resulting in a tighter DNA-histone interaction. This compaction of chromatin leads to the repression of transcription of DNA in that region.

特异性

Not tested with other species.
This antibody recognizes human HDAC7. Does not cross-react with HDAC1, HDAC4, or HDAC8.

免疫原

Epitope: a.a.164-182
Synthetic peptide corresponding to amino acids 164-182 of human HDAC7 [(C)KPKKSLERRKNPLLRKESA].

应用

Research Category
Epigenetics & Nuclear Function

Apoptosis & Cancer
Research Sub Category
Histones
Use Anti-HDAC7 Antibody (Rabbit Polyclonal Antibody) validated in WB to detect HDAC7 also known as histone deacetylase 7, histone deacetylase 7A.
Western Blotting:
A previous lot of this antibody was shown to recognize recombinant HDAC7 but not recombinant HDAC1, HDAC4, or HDAC8.

Western Blotting:
A previous lot of this antibody was shown to recognize endogenous HDAC7 in HEK293T cells.

质量

Routinely evaluated by Western blotting using recombinant HDAC7 protein.

目标描述

100 kDa

外形

Affinity purified
Purified Rabbit polyclonal in buffer containing 20 mM PBS and 0.1% sodium azide.

储存及稳定性

Stable for 1 year at 2-8ºC from date of receipt.

分析说明

Control
Recombinant HDAC7 protein (Cat. #14-832).

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

WGK 2

闪点(°F)

Not applicable

闪点(°C)

Not applicable


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Franck Dequiedt et al.
Immunity, 18(5), 687-698 (2003-05-20)
We report that HDAC7, a class II histone deacetylase, is highly expressed in CD4(+)CD8(+) double-positive thymocytes. HDAC7 inhibits the expression of Nur77, an orphan receptor involved in apoptosis and negative selection, via the transcription factor MEF2D. HDAC7 is exported from
Histone deacetylase inhibitors selectively suppress expression of HDAC7.
Dokmanovic, Milos, et al.
Molecular Cancer Therapeutics, 6, 2525-2534 (2007)
Chengzhuo Gao et al.
Molecular and cellular biology, 28(18), 5658-5667 (2008-07-16)
Promyelocytic leukemia protein (PML) sumoylation has been proposed to control the formation of PML nuclear bodies (NBs) and is crucial for PML-dependent cellular processes, including apoptosis and transcriptional regulation. However, the regulatory mechanisms of PML sumoylation and its specific roles
Yu-yi Lin et al.
Nature, 482(7384), 251-255 (2012-02-10)
First identified as histone-modifying proteins, lysine acetyltransferases (KATs) and deacetylases (KDACs) antagonize each other through modification of the side chains of lysine residues in histone proteins. Acetylation of many non-histone proteins involved in chromatin, metabolism or cytoskeleton regulation were further

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