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H3413

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-HD10
MDL number:
NACRES:
NA.41

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.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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This Item
H4539H8163H3159
conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

IgG fraction of antiserum

clone

polyclonal

clone

polyclonal

clone

polyclonal

clone

polyclonal

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

mol wt

antigen ~72 kDa

mol wt

antigen ~39 kDa

mol wt

antigen ~124 kDa

mol wt

antigen 55 kDa

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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.

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.

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.

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Dual role of HDAC10 in lysosomal exocytosis and DNA repair promotes neuroblastoma chemoresistance
Ridinger J, et al.
Scientific reports, 8(1), 10039-10039 (2018)
HDAC10 promotes lung cancer proliferation via AKT phosphorylation
Yang Y, et al.
Oncotarget, 7(37), 59388-59388 (2016)
Roles of histone deacetylases in epigenetic regulation: emerging paradigms from studies with inhibitors
Delcuve G, et al.
Clinical epigenetics, 4(1), 1-13 (2012)
Jenny J Tong et al.
Nucleic acids research, 30(5), 1114-1123 (2002-02-28)
Histone acetylation is important for regulating chromatin structure and gene expression. Three classes of mammalian histone deacetylases have been identified. Among class II, there are five known members, namely HDAC4, HDAC5, HDAC6, HDAC7 and HDAC9. Here we describe the identification
Baoyu Duan et al.
Oncotarget, 8(37), 61338-61349 (2017-10-06)
Angiogenesis is crucially involved in many physiological and pathological processes including tumor growth, but the molecular mechanisms regulating angiogenesis are incompletely understood. In this study, we investigated the functions and mechanism of histone deacetylase 10 (HDAC10), a member of the

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