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H2537

Sigma-Aldrich

Anti-Histone Deacetylase 7 (HDAC7) (YS-19) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~105 kDa

species reactivity

mouse, human, rat

technique(s)

immunoprecipitation (IP): 1.5-1.8 μg using RIPA extract of 293T cells expressing recombinant human HDAC7
microarray: suitable
western blot: 1:2,000 using whole extracts of mouse NIH-3T3 cells
western blot: 1:500 using whole extracts of rat PC12 cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HDAC7(51564)
mouse ... Hdac7(56233)
rat ... Hdac7a(84582)

General description

Histone deacetylases (HDACs) are competing enzymes, belonging to histone deacetylase family. There are two classes of HDACs with six to seven different types of HDACs proteins. HDAC1, HDAC2 and HDAC3 belong to Class I HDACs and HDAC4, HDAC6, and HDAC7 belong to Class II HDACs. Class I HDACs consists of a single deacetylase domain at the N-termini and diversified C-terminal regions, while Class II contains a deacetylase domain at C-terminal position. HDAC7 is predominantly found in the cell nucleus and slightly in cytoplasm. HDAC7 shuttles between these two regions and this is controlled by 14-3-3 protein and calmodulin-dependent kinase I (CaMKI)

Immunogen

synthetic peptide corresponding to amino acids 137-155 of mouse HDAC7 with N-terminal added lysine, conjugated to KLH.

Application

Anti-Histone Deacetylase 7 (HDAC7) (YS-19) antibody produced in rabbit has been used in:
  • immunoblotting
  • immunoprecipitation
  • antibody microarray

Biochem/physiol Actions

HDAC7 belongs to class II of HDAC family and combines with MEF2 group of transcription factors, which is facilitated by theN-terminal domain of HDAC7. This binding blocks the transcriptional activity and prevents myogenesis. They are involved in development and differentiation processes in various tissues such as skeletal, cardiac, and smooth muscle, the bone, the immune system, the vascular system, and the brain. These signal-dependent co-repressors phosporylate at the regulatory N-terminal domain resulting in nuclear export.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

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

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Identification of intracellular proteins and signaling pathways in human endothelial cells regulated by angiotensin-(1-7)
Meinert C, et al.
Journal of Proteomics, 130, 129-139 (2016)
W Fischle et al.
The Journal of biological chemistry, 276(38), 35826-35835 (2001-07-24)
Histone deacetylases (HDACs) are part of transcriptional corepressor complexes and play key roles in regulating chromatin structure. Three different classes of human HDACs have been defined based on their homology to HDACs found in Saccharomyces cerevisiae: RPD3 (class I), HDA1
H Y Kao et al.
The Journal of biological chemistry, 276(50), 47496-47507 (2001-10-05)
Here we show that HDAC7, a member of the class II histone deacetylases, specifically targets several members of myocyte enhancer factors, MEF2A, -2C, and -2D, and inhibits their transcriptional activity. Furthermore, we demonstrate that DNA-bound MEF2C is capable of recruiting
U Dressel et al.
The Journal of biological chemistry, 276(20), 17007-17013 (2001-03-30)
The overlapping expression profile of MEF2 and the class-II histone deacetylase, HDAC7, led us to investigate the functional interaction and relationship between these regulatory proteins. HDAC7 expression inhibits the activity of MEF2 (-A, -C, and -D), and in contrast MyoD
Further intracellular proteins and signaling pathways regulated by angiotensin-(1-7) in human endothelial cells
Meinert C, et al.
Data in Brief, 10, 354-363 (2017)

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