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H6287

Sigma-Aldrich

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

clone HDAC1-21, purified from hybridoma cell culture

Synonyme(s) :

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

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About This Item

Numéro MDL:
MFCD01633420
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

200

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

HDAC1-21, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~65 kDa

Espèces réactives

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

Numéro d'accès UniProt

Q13547

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

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

Actions biochimiques/physiologiques

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.

Forme physique

solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

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Consulter la Bibliothèque de documents

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)
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)
Engineering cell signaling using tunable CRISPR-Cpf1-based transcription factors
Liu Y, et al.
Nature Communications, 8(1), 2095-2095 (2017)
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
Hengxiang Cui et al.
Cancer science, 112(5), 1798-1810 (2021-02-26)
The G-protein-coupled receptor 126 (GPR126) may play an important role in tumor development, although its role remains poorly understood. We found that GPR126 had higher expression in most colorectal cancer cell lines than in normal colon epithelial cell lines, and
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