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Merck

H3413

Sigma-Aldrich

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

affinity isolated antibody, buffered aqueous solution

别名:

Anti-HD10

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About This Item

MDL號碼:
分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

rabbit

共軛

unconjugated

抗體表格

affinity isolated antibody

抗體產品種類

primary antibodies

無性繁殖

polyclonal

形狀

buffered aqueous solution

分子量

antigen ~72 kDa

物種活性

mouse, rat, human

技術

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登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

相关类别

一般說明

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.

免疫原

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

應用

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

生化/生理作用

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.

外觀

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

免責聲明

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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儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 2

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

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


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Polyamine Homeostasis in Snyder-Robinson Syndrome
Murray-ST, et al.
Medical sciences (Basel, Switzerland), 6(4), 112-112 (2018)
Dual role of HDAC10 in lysosomal exocytosis and DNA repair promotes neuroblastoma chemoresistance
Ridinger J, et al.
Scientific reports, 8(1), 10039-10039 (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.
Medical sciences (Basel, Switzerland), 6(4) (2018-12-14)
Loss-of-function mutations of the spermine synthase gene (SMS) result in Snyder-Robinson Syndrome (SRS), a recessive X-linked syndrome characterized by intellectual disability, osteoporosis, hypotonia, speech abnormalities, kyphoscoliosis, and seizures. As SMS catalyzes the biosynthesis of the polyamine spermine from its precursor
Annunziata Gloghini et al.
British journal of haematology, 147(4), 515-525 (2009-09-25)
Unselective histone deacetylase (HDAC) inhibitors are a promising novel therapy for lymphoid malignancies. However, these treatments remain empiric as the pattern of HDAC enzymes in different types of cancer, including lymphoid malignancies, remains unknown. We examined the expression of class

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