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H0913

Sigma-Aldrich

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

clone AH3-120, purified from hybridoma cell culture

Sinônimo(s):

Anti-H3K9ac

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

mouse

Nível de qualidade

conjugado

unconjugated

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

AH3-120, monoclonal

forma

buffered aqueous solution

peso molecular

antigen ~17 kDa

reatividade de espécies

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

embalagem

antibody small pack of 25 μL

concentração

~2 mg/mL

técnica(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

Isotipo

IgG1

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

acetylation (Lys9)

Descrição geral

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.

Imunogênio

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.

Aplicação

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

Ações bioquímicas/fisiológicas

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.

forma física

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

Exoneração de responsabilidade

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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Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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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)
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
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)

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