H9286

Anti-acetyl-Histone H3 (Ac-Lys⁹) antibody produced in rabbit

Name: Anti-acetyl-Histone H3 (Ac-Lys<SUP>9</SUP>) antibody produced in rabbit
Brand: SIGMA

2-2.5 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-H3K9ac

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About This Item

UNSPSC Code:

12352203

NACRES:

NA.41

MDL number:

MFCD02685921

Product Name

Anti-acetyl-Histone H3 (Ac-Lys⁹) antibody produced in rabbit, 2-2.5 mg/mL, affinity isolated antibody, buffered aqueous solution

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~17 kDa

species reactivity

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

concentration

2-2.5 mg/mL

technique(s)

indirect immunofluorescence: 1:1,000 using NIH3T3 mouse fibroblast cell line treated with sodium butyrate
microarray: suitable
western blot: 1:1,000 using whole cell extract of the mouse fibroblast NIH3T3 cell line treated with sodium butyrate

UniProt accession no.

P68431

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

acetylation (Lys9)

Quality Level

200

Application

Anti-acetyl-Histone H3 (Ac-Lys9) antibody produced in rabbit has been used in:

indirect immunofluorescence
immunoblotting
immunohistochemistry

Biochem/physiol Actions

Histone proteins H3, H4, H2A, and H2B function as building blocks to package eukaryotic DNA into repeating nucleosome units that are folded in higher order chromatin fibers.

In most species, histone H3 is primarily acetylated at lysine 9, 14, 18, and 23. Acetylation at lysine 9 significantly influences histone deposition and chromatin assembly in some organisms. Acetylation of specific lysine residues in H3 is also associated with processes apart from transcription.

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.

General description

Anti-acetyl-Histone H3 (Ac-Lys9) antibody produced in rabbit is suitable for:

indirect immunofluorescence at a dilution of 1:1,000 using NIH3T3 mouse fibroblast cell line treated with sodium butyrate
microarray
western blot at a dilution of 1:1,000 using whole cell extract of the mouse fibroblast NIH3T3 cell line treated with sodium butyrate

Immunogen

synthetic acetylated [Ac-Lys⁹] histone H3 peptide (amino acids 7-20) 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.

Physical form

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

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Storage Class

12 - Non Combustible Liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number

0000510782

0000462431

0000232746

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Social isolation-induced epigenetic changes in midbrain of adult mice

Siuda D, et al.

Journal of Physiology And Pharmacology, 65(2), 247-255 (2014)

p66shc negatively regulates insulin-like growth factor I signal transduction via inhibition of p52shc binding to Src homology 2 domain-containing protein tyrosine phosphatase substrate-1 leading to impaired growth factor receptor-bound protein-2 membrane recruitment.

Gang Xi et al.

Molecular endocrinology (Baltimore, Md.), 22(9), 2162-2175 (2008-07-09)

Our previous studies have indicated an essential role of p52shc in mediating IGF-I activation of MAPK in smooth muscle cells (SMC). However, the role of the p66 isoform of shc in IGF-I signal transduction is unclear. In the current study

Nejire/dCBP-mediated histone H3 acetylation during spermatogenesis is essential for male fertility in Drosophila melanogaster.

Tim Hundertmark et al.

PloS one, 13(9), e0203622-e0203622 (2018-09-08)

Spermatogenesis in many species including Drosophila melanogaster is accompanied by major reorganisation of chromatin in post-meiotic stages, involving a nearly genome-wide displacement of histones by protamines, Mst77F and Protamine-like 99C. A proposed prerequisite for the histone-to-protamine transition is massive histone

Epigenetic stability in the adult mouse cortex under conditions of pharmacologically induced histone acetylation.

Jamie Benoit et al.

Brain structure & function, 221(8), 3963-3978 (2015-11-04)

Histone acetylation is considered a major epigenetic process that affects brain development and synaptic plasticity, as well as learning and memory. The transcriptional effectors and morphological changes responsible for plasticity as a result of long-term modifications to histone acetylation are

Histone H4 acetylation is essential to proceed from a histone- to a protamine-based chromatin structure in spermatid nuclei of Drosophila melanogaster.

Stephan Awe et al.

Systems biology in reproductive medicine, 56(1), 44-61 (2010-02-23)

In humans, other mammals, and also in Drosophila, the paternal genome in the sperm is highly condensed and organized mainly in a protamine-based chromatin structure. However, the timing and mechanism of the switch from a histone- to the protamine-based chromatin

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Anti-acetyl-Histone H3 (Ac-Lys9) antibody produced in rabbit