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Merck

H3413

Anti-Histone Deacetylase 10 (HDAC10) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-HD10

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A propos de cet article

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
MFCD06201937

Principaux documents

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Nom du produit

Anti-Histone Deacetylase 10 (HDAC10) 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 ~72 kDa

species reactivity

mouse, rat, human

technique(s)

indirect immunofluorescence: 10-20 μg/mL using human HeLa cells
microarray: suitable
western blot (chemiluminescent): 0.5-1.0 μg/mL using whole extracts of mouse NIH3T3 and rat NRK cells

UniProt accession no.

Q969S8

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

200

Gene Information

human ... HDAC10(83933)
mouse ... Hdac10(170787)
rat ... Hdac10(362981)

Catégories apparentées

Application

Anti-Histone Deacetylase 10 (HDAC10) antibody produced in rabbit has been used in western blot analysis and immunofluorescence.

Biochem/physiol Actions

Histone deacetylase 10 (HDAC10) can deacetylate histones, repress transcription and interact with HDAC3. HDAC10 can stimulate lung cancer proliferation via AKT phosphorylation. It is involved in homologous recombination.
The leucine-rich domain on the C-terminal of HDAC8 is responsible for cytoplasmic enrichment. Trichostatin A (TSA), a specific antitumor deacetylase inhibitor is sensitive to the enzymatic activity of HDAC10. HDAC10 attaches to a promoter and represses transcription in the nucleas.

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

Histone deacetylase 10 (HDAC10) is highly expressed in liver, kidney, pancreas and spleen. HDAC10 is similar to HDAC6, both containing a unique putative second catalytic domain not found in other HDACs. HDAC10 is localized to both the nucleus and cytoplasm. Histone deacetylases (HDACs) are competing enzymes, belonging to histone deacetylase family. HDAC10 is a novel member of the class II family of HDACs with a bipartite structure consisting of Hda1p-related catalytic domain at the N-terminal and a leucine-rich domain at the C-terminal. It is present, both in the nucleas and cytoplasm.

Immunogen

synthetic peptide corresponding to amino acid residues 2-16 of human HDAC10 with C-terminal added cysteine, conjugated to KLH.

Physical form

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

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Classe de stockage

10 - Combustible liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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Certificats d'analyse (COA)

Lot/Batch Number
0000394491
0000394491
0000245451
0000235797
0000245451

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Consulter la Bibliothèque de documents

Polyamine Homeostasis in Snyder-Robinson Syndrome
Murray-ST, et al.
Medical sciences (Basel, Switzerland), 6(4), 112-112 (2018)
Salma Darwish et al.
International journal of molecular sciences, 23(14) (2022-07-28)
In addition to involvement in epigenetic gene regulation, histone deacetylases (HDACs) regulate multiple cellular processes through mediating the activity of non-histone protein substrates. The knockdown of HDAC8 isozyme is associated with the inhibition of cell proliferation and apoptosis enhancement in
Roles of histone deacetylases in epigenetic regulation: emerging paradigms from studies with inhibitors
Delcuve G, et al.
Clinical epigenetics, 4(1), 1-13 (2012)
HDAC10 promotes lung cancer proliferation via AKT phosphorylation
Yang Y, et al.
Oncotarget, 7(37), 59388-59388 (2016)
Tracy Murray Stewart et al.
The Journal of biological chemistry, 298(10), 102407-102407 (2022-08-22)
Cytosolic histone deacetylase-10 (HDAC10) specifically deacetylates the modified polyamine N8-acetylspermidine (N8-AcSpd). Although intracellular concentrations of N8-AcSpd are low, extracellular sources can be abundant, particularly in the colonic lumen. Extracellular polyamines, including those from the diet and microbiota, can support tumor
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