H3413
Anti-Histone Deacetylase 10 (HDAC10) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-HD10
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About This Item
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 ~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
human ... HDAC10(83933)
mouse ... Hdac10(170787)
rat ... Hdac10(362981)
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.
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WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
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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Find documentation for the products that you have recently purchased in the Document Library.
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
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
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
Dual role of HDAC10 in lysosomal exocytosis and DNA repair promotes neuroblastoma chemoresistance
Ridinger J, et al.
Scientific reports, 8(1), 10039-10039 (2018)
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