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Merck

H0913

Sigma-Aldrich

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

clone AH3-120, purified from hybridoma cell culture

Synonym(e):

Anti-H3K9ac

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

AH3-120, monoclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~17 kDa

Speziesreaktivität

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

Verpackung

antibody small pack of 25 μL

Konzentration

~2 mg/mL

Methode(n)

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

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

acetylation (Lys9)

Allgemeine Beschreibung

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.

Immunogen

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.

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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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Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

WGK 2

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

A novel Arabidopsis acetyltransferase interacts with the geminivirus movement protein NSP
McGarry RC, et al.
Plant Cell, 15, 1605-1618 (2003)
Farnoosh Jafarpour et al.
International journal of fertility & sterility, 4(4), 148-155 (2011-01-01)
Reconstructed embryos from terminally differentiated somatic cells have revealed high levels of genomic methylation which results in inappropriate expression patterns of imprinted and non-imprinted genes. These aberrant expressions are probably responsible for different abnormalities during the development of clones. Improvement
Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae
Hyland EM, et al.
Molecular and Cellular Biology, 25, 10060-10070 (2005)
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)
Regulation of immune responses by histone deacetylase inhibitor
Licciardi PV and Karagiannis TC
ISRN hematology, 2012 (2012)

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