07-595
Anti-acetyl-Histone H4 (Lys12) Antibody
serum, Upstate®
Synonym(s):
H4K12Ac, Histone H4 (acetyl K12)
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Product Name
Anti-acetyl-Histone H4 (Lys12) Antibody, serum, Upstate®
biological source
rabbit
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
Saccharomyces cerevisiae, human
manufacturer/tradename
Upstate®
technique(s)
ChIP: suitable (ChIP-seq)
dot blot: suitable
western blot: suitable
isotype
IgG
NCBI accession no.
shipped in
dry ice
target post-translational modification
acetylation (Lys12)
Quality Level
Gene Information
human ... HIST2H4B(554313)
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Analysis Note
Control
Acid extracted proteins from HeLa cells treated with sodium butyrate
Acid extracted proteins from HeLa cells treated with sodium butyrate
routinely evaluated by immunoblot on acid extracted proteins from HeLa cells
Application
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Histones
Histones
Use Anti-acetyl-Histone H4 (Lys12) Antibody (Rabbit Polyclonal Antibody) validated in ChIP, DB, WB, ChIP-seq to detect acetyl-Histone H4 (Lys12) also known as H4K12Ac, Histone H4 (acetyl K12).
Biochem/physiol Actions
Broad species cross-reactivity expected
Recognizes Histone H4 acetylated on lysine 12.
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
10 kDa
Histone H4 is one of the 5 main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N terminal tail H4 is involved with the structure of the nucleosomes of the ′beads on a string′ structure.
Acetylation of histone H4 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as Histone Acetyl Transferases (HATs).
Acetylation of histone H4 occurs at several different lysine positions in the histone tail and is performed by a family of enzymes known as Histone Acetyl Transferases (HATs).
Immunogen
peptide containing the sequence (LGAcKGG) corresponding to lysine 12 acetylation of yeast Histone H4.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Physical form
Depleted rabbit antiserum in 30% glycerol, 0.07M Tris-glycine, pH 7.4, 0.105 M NaCl, 0.035% sodium azide as a preservative.
Immunodepleted Serum
Preparation Note
Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
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Storage Class
10 - Combustible liquids
wgk
WGK 1
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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Find documentation for the products that you have recently purchased in the Document Library.
The molecular topography of silenced chromatin in Saccharomyces cerevisiae.
Thurtle, DM; Rine, J
Genes & Development null
The complex pattern of epigenomic variation between natural yeast strains at single-nucleosome resolution.
Filleton, F; Chuffart, F; Nagarajan, M; Bottin-Duplus, H; Yvert, G
Epigenetics & Chromatin null
Paola Y Bertucci et al.
Nucleic acids research, 41(12), 6072-6086 (2013-05-04)
Steroid receptors were classically described for regulating transcription by binding to target gene promoters. However, genome-wide studies reveal that steroid receptors-binding sites are mainly located at intragenic regions. To determine the role of these sites, we examined the effect of
Panagis Filippakopoulos et al.
Cell, 149(1), 214-231 (2012-04-03)
Bromodomains (BRDs) are protein interaction modules that specifically recognize ε-N-lysine acetylation motifs, a key event in the reading process of epigenetic marks. The 61 BRDs in the human genome cluster into eight families based on structure/sequence similarity. Here, we present
Histone deacetylase inhibitors modify pancreatic cell fate determination and amplify endocrine progenitors.
Haumaitre, Cecile, et al.
Molecular and cellular biology, 28, 6373-6383 (2008)
Global Trade Item Number
| SKU | GTIN |
|---|---|
| 07-595 | 04053252733284 |
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