Peptide corresponding to Histone H4 containing the sequence [GRG-AcK-GGK] on which Lys5 is acetylated.
Application
Detect acetyl-Histone H4 (Lys5) using this Anti-acetyl-Histone H4 (Lys5) Antibody, rabbit validated for use in WB.
Research Category Epigenetics & Nuclear Function
Research Sub Category Histones
Quality
Routinely evaluated by immunoblot.
Target description
11kDa
Physical form
100 μL of rabbit monoclonal IgG cell culture supernatant in 0.1% sodium azide.
Storage and Stability
2 years at -20°C from date of shipment
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Journal of experimental & clinical cancer research : CR, 21(3), 377-382 (2002-10-19)
Acetylation of core histones is closely linked to transcriptional activation of various genes. The acetylation levels of nucleosomal histones can be modified through a balance of histone acetyltransferases and deacetylases. To elucidate the role of histone acetylation in human gastric
RSC exploits histone acetylation to abrogate the nucleosomal block to RNA polymerase II elongation.
Context-dependent dynamic histone modifications constitute a key epigenetic mechanism in gene regulation1-4. The Rpd3 small (Rpd3S) complex recognizes histone H3 trimethylation on lysine 36 (H3K36me3) and deacetylates histones H3 and H4 at multiple sites across transcribed regions5-7. Here we solved
Epigenetic chromatin modifications in barley after mutagenic treatment.
Braszewska-Zalewska, A; Tylikowska, M; Kwasniewska, J; Szymanowska-Pulka, J
Journal of molecular biology, 422(4), 556-574 (2012-06-13)
We recently documented the co-purification of members of the LIV-1 subfamily of ZIP (Zrt-, Irt-like Protein) zinc transporters (LZTs) with the cellular prion protein (PrP(C)) and, subsequently, established that the prion gene family descended from an ancestral LZT gene. Here
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