H2662
Anti-Histone Deacetylase 7 (HDAC7) (KG-17) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
别名:
Anti-HD7, Anti-HD7A, Anti-HDAC7A
产品名称
Anti-Histone Deacetylase 7 (HDAC7) (KG-17) antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
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.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... HDAC7(51564)
mouse ... Hdac7(56233)
rat ... Hdac7a(84582)
Application
Anti-Histone Deacetylase 7 (HDAC7) (KG-17) antibody produced in rabbit has been used in
- indirect immunofluorescene
- immunoblotting
- immunoprecipitation
Biochem/physiol Actions
Anti-Histone Deacetylase 7 recognizes human, mouse, and rat HDAC7.
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).
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
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.
Immunogen
Synthetic peptide corresponding to amino acids of human HDAC7, conjugated to KLH.
Physical form
Solution in 0.01 M phosphate buffered saline containing 1% bovine serum albumin and 15 mM sodium azide.
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存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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)
Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor
Lemercier C, et al.
Test, 277(24), 22045-22052 (2002)
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)
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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