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H6287

Sigma-Aldrich

Anti-Histone Deacetylase 1 (HDAC1) antibody, Mouse monoclonal

clone HDAC1-21, purified from hybridoma cell culture

Synonym(s):

Monoclonal Anti-Histone Deacetylase 1 (HDAC1) antibody produced in mouse

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About This Item

MDL number:
MFCD01633420
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

HDAC1-21, monoclonal

form

buffered aqueous solution

mol wt

antigen ~65 kDa

species reactivity

mouse, human

concentration

~2 mg/mL

technique(s)

immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 2-4 μg/mL using total cell extracts of HeLa cells

isotype

IgG3

UniProt accession no.

Q13547

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HDAC1(3065)
mouse ... Hdac1(433759)

Related Categories

General description

Anti-Histone Deacetylase 1 (HDAC1) antibody, Mouse monoclonal (mouse IgG3 isotype) is derived from the HDAC1-21 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to amino acids of human and mouse histone deacetylase 1 (HDAC1).
Histone deacetylases (HDACs) are competing enzymes, belonging to histone deacetylase family. There are two classes of HDACs with six to seven different types of HDACs proteins. HDAC1,HDAC2 and HDAC3 belong to Class I HDACs and HDAC4, HDAC6, and HDAC7 belong to Class II HDACs. Class I HDACs consists of a single deacetylase domain at the N-termini and diversified C-terminal regions, while Class II contains a deacetylase domain at C-terminal position.

Application

Anti-Histone Deacetylase 1 (HDAC1) antibody, Mouse monoclonal has been used in:
  • enzyme-linked immunosorbent assay (ELISA)
  • immunoprecipitation
  • immunoblotting

Biochem/physiol Actions

HDAC1 is widely studied and is shown to actively modulate the eukaryotic chromatin structure. It deacetylyses lysine residues on core histones (H2A, H2B, H3 and H4) at the N-terminal. It is a vital component of cofactor complexes and is involved in transcription regulation. Histone deacetylation results in transcription repression leading to the formation of tight nucleosomal structure which prevents DNA accessing.

Physical form

solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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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Stem cell factor SALL4 represses the transcriptions of PTEN and SALL1 through an epigenetic repressor complex
Lu J, et al.
PLoS ONE, 4(5), e5577-e5577 (2009)
Zhanguo Gao et al.
The Journal of biological chemistry, 281(7), 4540-4547 (2005-12-24)
Inhibition of peroxisome proliferator-activated receptor gamma (PPARgamma) function by TNF-alpha contributes to glucose and fatty acid metabolic disorders in inflammation and cancer, although the molecular mechanism is not fully understood. In this study, we demonstrate that nuclear translocation of HDAC3
Sudhakar Ammanamanchi et al.
The Journal of biological chemistry, 278(37), 35775-35780 (2003-07-03)
Sp3 transcription factor can either activate or repress target gene expression. However, the molecular event that controls this dual function is unclear. We previously reported (Ammanamanchi, S., and Brattain, M. G. (2001) J. Biol. Chem. 276, 3348-3352) that unmodified Sp3
Coactivators and corepressors of NF-kappaB in IkappaB alpha gene promoter
Gao Z, et al.
The Journal of biological chemistry, 280(22), 21091-21098 (2005)
Qing He et al.
American journal of physiology. Endocrinology and metabolism, 300(5), E877-E885 (2011-02-24)
The transcription factor HIF-1α activity is increased in adipose tissue to contribute to chronic inflammation in obesity. However, its upstream and downstream events remain to be characterized in adipose tissue in obesity. We addressed this issue by investigating adipocyte HIF-1α
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