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H0788

Sigma-Aldrich

Monoclonal Anti-acetyl- & phospho-Histone H3 (Ac-Lys9, pSer10) antibody produced in mouse

~2 mg/mL, clone APH3-64, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-H3K9acS10p

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

APH3-64, monoclonal

form

buffered aqueous solution

mol wt

antigen ~17 kDa

species reactivity

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

concentration

~2 mg/mL

technique(s)

immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: suitable using whole cell extract of Jurkat cell line treated with nocodazole

isotype

IgG2a

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

acetylation (Lys9), phosphorylation (pSer10)

General description

Monoclonal Anti-Acetyl & Phospho-Histone H3 (Ac-Lys9, pSer10) (mouse IgG2a isotype) is derived from the APH3-64 hybridoma produced by the fusion of mouse myeloma cells (NS1) and splenocytes from BALB/c mice immunized with a synthetic, acetylated and phosphorylated histone H3 peptide. Histone H3 is a component of the histone octamer of the nucleosome DNA complex. It possesses a lysine-rich N-terminal tail region.

Specificity

Monoclonal Anti-Acetyl & Phospho-Histone H3 (Ac-Lys, pSer) specifically recognizes human histone H3 only when simultaneously acetylated on Lys and phosphorylated at Ser.

Immunogen

synthetic, acetylated and phosphorylated histone H3 peptide (amino acids 7-20, Ac-Lys9, pSer10) corresponding to the N-terminus of human histone H3. The sequence is identical in many species.

Application

Monoclonal Anti-acetyl- & phospho-Histone H3 (Ac-Lys9, pSer10) antibody produced in mouse has been used in:
  • chromatin immunoprecipitation
  • antibody microarray
  • enzyme-linked immunosorbent assay (ELISA)
  • immunoblotting
  • immunoprecipitation

Biochem/physiol Actions

Acetylation of histones on lysine residues within the N-terminal domain by histone acetyl-transferase (HATs) including histone acetyltransferase (Gcn5p), p300/CREB-binding protein-associated factor (P/CAF), E1A binding protein p300/CREB-binding protein (p300/CBP), and transcription initiation factor TFIID 250 kDa subunit (TAFII250) is associated with transcriptional activation. This modification results in remodeling of the nucleosome structure making it more accessible to transcription complexes. In most species, histone H3 is primarily acetylated at lysines 9, 14, 18, and 23. In some organisms, acetylation at lysine 9 appears to have a dominant role in histone deposition and chromatin assembly. Phosphorylation of histone H3 on Ser10 is tightly correlated with chromosome condensation during both mitosis and meiosis. Phosphorylation at serine is implicated with the induction of immediate-early oncogenes like c-jun, c-fos, and c-myc. Protein kinase A (PKA), 90 kDa ribosomal S6 kinase-2 (Rsk-2), and MAP- and Stress-activated kinase 1 (Msk-1) are necessary for histone H3 phosphorylation. The ERK and p38 pathways activate Msk-1 to phosphorylate histone H3. Monoclonal antibodies to acetylated and phosphorylated histone H3 are an important tool for studying chromatin remodeling and gene regulation.

Physical form

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

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots at −20 °C. Repeated freezing and thawing is not recom-mended. Storage in “frost-free” freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Christian Meinert et al.
Data in brief, 10, 354-363 (2016-12-27)
In 2016, Meinert et al. (doi: 10.1016/j.jprot.2015.09.020) published the first 25 proteins in a protein array regulated in Human Umbilical Vein Endothelial Cells (HUVEC) by the heptapeptide angiotensin (Ang)-(1-7) and the first 10 intracellular signaling cascades at different time points.
D E Sterner et al.
Microbiology and molecular biology reviews : MMBR, 64(2), 435-459 (2000-06-06)
The state of chromatin (the packaging of DNA in eukaryotes) has long been recognized to have major effects on levels of gene expression, and numerous chromatin-altering strategies-including ATP-dependent remodeling and histone modification-are employed in the cell to bring about transcriptional
Signaling to chromatin through histone modifications.
P Cheung et al.
Cell, 103(2), 263-271 (2000-11-01)
Anne-Marie Baird et al.
PloS one, 6(1), e14593-e14593 (2011-02-08)
Angiogenesis may play a role in the pathogenesis of Non-Small Cell Lung cancer (NSCLC). The CXC (ELR(+)) chemokine family are powerful promoters of the angiogenic response. The expression of the CXC (ELR(+)) family members (CXCL1-3/GROα-γ, CXCL8/IL-8, CXCR1/2) was examined in
B D Strahl et al.
Nature, 403(6765), 41-45 (2000-01-19)
Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of

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