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H2662

Sigma-Aldrich

Anti-Histone Deacetylase 7 (HDAC7) (KG-17) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-HD7, Anti-HD7A, Anti-HDAC7A
MDL number:
MFCD04040364
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

200

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): 1.0-1.5 μg using RIPA extract of 293T cells expressing recombinant human HDAC7
indirect immunofluorescence: 1:50 using rat NRK cells
western blot: 1:1,000 using whole extracts of mouse NIH-3T3 cells

UniProt accession no.

Q8WUI4

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

Mammalian histone deacetylases (HDACs) can be divided into three classes according to sequence homology. Class I consists of the yeast transcriptional regulatory protein Rpd3-like proteins HDAC1, HDAC2, HDAC3, and HDAC8. Class II consists of the yeast Hda1-like proteins HDAC4, HDAC5, HDAC6, HDAC7, HDAC9 and HDAC10. Class III consists of the yeast sirtuin 2 (Sir2)-like proteins. Although HDAC7 is localized mostly to the cell nucleus, it is also found in the cytoplasm.

Specificity

Anti-Histone Deacetylase 7 recognizes human, mouse, and rat HDAC7.

Immunogen

Synthetic peptide corresponding to amino acids of human HDAC7, conjugated to KLH.

Application

Anti-Histone Deacetylase 7 (HDAC7) (KG-17) antibody produced in rabbit has been used in
  • indirect immunofluorescene
  • immunoblotting
  • immunoprecipitation

Biochem/physiol Actions

Class II histone deacetylases (HDACs) have been implicated in the regulation of muscle differentiation. Interaction of HDAC4, -5, and -7 with members of the myocyte enhancer factor-2 (Mef2) family of transcription factors represses their transcriptional activity and prevents myogenesis. Shuttling of HDAC7 between the cell nucleus and the cytoplasm is controlled by a mechanism involving calmodulin independent kinase I (CaMKI) and 14-3-3 proteins. The HDAC7 enzymatic activity depends on its interaction with the class I HDAC3, and the corepressors silencing mediator of retinoic acid and thyroid hormone receptors (SMRT) and nuclear receptor co-repressor (N-COR). HDAC7 also interacts with the transcriptional repressor B-cell lymphoma 6 (BCL-6).

Physical form

Solution in 0.01 M phosphate buffered saline 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.

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品
含少量动物源组分生物产品

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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Splicing of HDAC7 modulates the SRF-myocardin complex during stem-cell differentiation towards smooth muscle cells
Margariti A, et al.
Journal of Cell Science, 122(4), 460-470 (2009)
Erasers of histone acetylation: the histone deacetylase enzymes
Seto E and Yoshida M
Cold Spring Harbor Perspectives in Biology, 6(4), a018713-a018713 (2014)
Human HDAC7 Histone Deacetylase Activity Is Associated with HDAC3in Vivo
Fischle W, et al.
Test, 276(38), 35826-35835 (2001)
Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor
Lemercier C, et al.
Test, 277(24), 22045-22052 (2002)
Carina Mello Guimaraes Meyers et al.
Bone, 159, 116393-116393 (2022-03-24)
Protein kinase D (PRKD) family kinases are required for formation and function of osteoclasts. However, the substrates of PRKD in osteoclasts are unknown. To identify PRKD-dependent protein phosphorylation in osteoclasts, we performed a quantitative LC-MS/MS phosphoproteomics screen for proteins showing
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