产品名称
Anti-HDAC7 Antibody, from rabbit, purified by affinity chromatography
biological source
rabbit
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
human
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... HDAC7(51564)
Analysis Note
Control
Recombinant HDAC7 protein (Cat. #14-832).
Recombinant HDAC7 protein (Cat. #14-832).
Routinely evaluated by Western blotting using recombinant HDAC7 protein.
Application
Research Category
Epigenetics & Nuclear Function
Apoptosis & Cancer
Epigenetics & Nuclear Function
Apoptosis & Cancer
Research Sub Category
Histones
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.
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.
Biochem/physiol Actions
Not tested with other species.
This antibody recognizes human HDAC7. Does not cross-react with HDAC1, HDAC4, or HDAC8.
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.
General description
100 kDa
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.
Immunogen
Epitope: a.a.164-182
Synthetic peptide corresponding to amino acids 164-182 of human HDAC7 [(C)KPKKSLERRKNPLLRKESA].
Physical form
Affinity purified
Purified Rabbit polyclonal in buffer containing 20 mM PBS and 0.1% sodium azide.
Preparation Note
Stable for 1 year at 2-8ºC from date of receipt.
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存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Histone deacetylase inhibitors selectively suppress expression of HDAC7.
Dokmanovic, Milos, et al.
Molecular Cancer Therapeutics, 6, 2525-2534 (2007)
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
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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