acetyl-Histone H3 (Lys18) Monoclonal Antibody ChIP Grade


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Cat.No.:  EAb-0534
Product Name:  acetyl-Histone H3 (Lys18) Monoclonal Antibody ChIP Grade
Description:  The mouse-derived antibody is purified with protein G-conjugated agarose followed by acetylated histone H3 (Lys18) peptide affinity chromatography. It specifically recognizes histone H3 with acetylation at Lys18.
Antibody Type:  Monoclonal
Immunogen:  Synthetic acetyl peptide corresponding to residues surrounding Lys18 of human histone H3
Host:  Mouse
Isotype:  IgG
Specificity:  H3 with acetylation at Lys18
Purification:  Antibodies are purified by protein G-conjugated agarose followed by acetylated histone H3 (Lys18) peptide affinity chromatography.
Appearance:  Liquid
Applications:  ChIP, IP
Recommended Dilutions/Conditions:  IP: 1:25; ChIP: 1:50
Recommended dilutions/conditions may not be available for all applications. Specific conditions for reactivity should be optimized by the end user.
Species Reactivity:  Eukaryotes
Storage:  -20°C
Storage Buffer:  PBS with 50% glycerol and 0.01% sodium azide.
Warning:  For Research Use Only! Not For Use in Humans.
Scientific Background:  The ε-amino lysine acetylation of proteins is an important reversible modification controlling protein activity. The amino-terminal tails of core histones undergo lysine acetylation in multiple sites, termed as “histone code”. Lysine acetylation in core histones occurs in response to various stimuli. It plays vital roles in the regulation of many cellular processes including chromatin dynamics, transcriptional activities, cell cycle progression, apoptosis, differentiation, and nuclear import.. In most species, histone H2A is primarily acetylated at Lys5, 9, 15, and 36; H2B is primarily acetylated at Lys5, 12, 15, 16, and 20. Histone H2B is primarily acetylated at Lys5, 9, 14, 18, 23, 27, 56, and 79. Histone H4 is primarily acetylated at Lys5, 8, 12, 16, and 20. More than 20 histone acetyltransferases (HATs) and 18 histone deacetylases (HDACs) have been identified to date, while the mechanistic details of substrate selection and site specificity of these enzymes remain unclear. The level of histone lysine acetylation has been found to be impaired in cancers and other diseases, therefore, enzymes regulating histone lysine acetylation have become promising targets for anti-cancer drugs.

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For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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