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H0913

Sigma-Aldrich

Anti-acetyl-Histone H3 (Ac-Lys9) antibody, Mouse monoclonal

clone AH3-120, purified from hybridoma cell culture

Synonyme(s) :

Anti-H3K9ac

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About This Item

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

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

AH3-120, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~17 kDa

Espèces réactives

human, bovine, Caenorhabditis elegans, frog, Drosophila, chicken, rat, mouse

Conditionnement

antibody small pack of 25 μL

Concentration

~2 mg/mL

Technique(s)

immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 1-2 μg/mL using whole cell extract of mouse fibroblasts 3T3 cell line treated with sodium butyrate

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

acetylation (Lys9)

Description générale

Monoclonal Anti-Acetyl-Histone H3 (Ac-Lys9) recognizes human histone H3 when acetylated on Lys9. Staining of the histone H3-Ac-Lys9 band in immunoblotting is specifically inhibited with the acetylated histone H3 immunizing peptide but not with the nonacetylated one.

Immunogène

synthetic, acetylated histone H3 peptide (amino acids 7-20, Ac-Lys9) corresponding to the N-terminus of human histone H3. The sequence is identical in many species including mouse, rat, bovine, chicken, frog, Drosophila, and C. elegans, and is highly conserved (single amino acid substitution) in Tetrahymena histone H3.

Application

Monoclonal Anti-acetyl-Histone H3 (Ac-Lys9) antibody may be used in various applications including ELISA, immunoblotting (approx. 17 kDa), and immunocytochemistry.

Actions biochimiques/physiologiques

Acetyl-Histone H3 hav Acetylation of lysine residues within these N-terminal domains of histones by histone acetyl-transferase (HATs), including Gcn5p, PCAF, p300/CBP and TAFII250 is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure into an open conformation more accessible to transcription complexes. Conversely, histone deacetylation by histone deacetylase (HDACs) is associated with transcription repression reversing the chromatin remodeling process. In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. Acetylation of specific lysines in histone H3 is also associated with processes apart from transcription. During DNA replication, new histones are rapidly synthesized and assembled into replicated DNA. Histones H3 and H4 are brought to replicating chromatin in a pre-acetylated state that turns into a de-acetylated state after replication is completed and the newly assembled chromatin matures.

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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Produit(s) apparenté(s)

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Regulation of immune responses by histone deacetylase inhibitor
Licciardi PV and Karagiannis TC
ISRN hematology, 2012 (2012)
Priyanka Jain et al.
Scientific reports, 9(1), 8508-8508 (2019-06-13)
Glycosylphosphatidylinositol (GPI)-anchored proteins are important for virulence of many pathogenic organisms including the human fungal pathogen, Candida albicans. GPI biosynthesis is initiated by a multi-subunit enzyme, GPI-N-acetylglucosaminyltransferase (GPI-GnT). We showed previously that two GPI-GnT subunits, encoded by CaGPI2 and CaGPI19
A novel Arabidopsis acetyltransferase interacts with the geminivirus movement protein NSP
McGarry RC, et al.
Plant Cell, 15, 1605-1618 (2003)
Histone H3 variants and modifications on transcribed genes
Workman JL and Abmayr SM
Proceedings of the National Academy of Sciences of the USA, 101, 1429-1430 (2004)
Prabakaran Nagarajan et al.
PLoS genetics, 9(6), e1003518-e1003518 (2013-06-12)
Histone acetyltransferase 1 is an evolutionarily conserved type B histone acetyltransferase that is thought to be responsible for the diacetylation of newly synthesized histone H4 on lysines 5 and 12 during chromatin assembly. To understand the function of this enzyme

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