histone acetylation and methylation

By Targets:	Histone Methyltransferase (2)
By Research Areas:	Cancer (2)

Targets Recommended: Histone Methyltransferase Histone Demethylase Histone Acetyltransferase HDAC Fat Mass and Obesity-associated Protein (FTO)

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-163593

PRMT5-IN-44	Histone Methyltransferase	Cancer
PRMT5-IN-44 (compound 12) is a PRMT5 inhibitor. PRMT5-IN-44 can be used in cancer research .

HY-163592

PRMT5-IN-43	Histone Methyltransferase	Cancer
PRMT5-IN-43 (compound 4A) is a PRMT5 inhibitor. PRMT5-IN-43 can be used in cancer research .

Cat. No.	Product Name

HY-L024

Histone Modification Research Compound Library	621 compounds
A histone modification, a covalent post-translational modification (PTM) to histone proteins, includes methylation, phosphorylation, acetylation, ubiquitylation, and sumoylation, etc. In general, histone modifications are catalyzed by specific enzymes that act predominantly at the histone N-terminal tails involving amino acids such as lysine or arginine, as well as serine, threonine, tyrosine, etc. The PTMs made to histones can impact gene expression by altering chromatin structure or recruiting histone modifiers. Histone modifications act in diverse biological processes such as transcriptional activation/inactivation, chromosome packaging, and DNA damage/repair. Deregulation of histone modification contributes to many diseases, including cancer and autoimmune diseases. MCE owns a unique collection of 621 bioactive compounds targeting Epigenetic Reader Domain, HDAC, Histone Acetyltransferase, Histone Demethylase, Histone Methyltransferase, Sirtuin, etc. Histone Modification Research Compound Library is a useful tool for histone modification research and drug screening.

Histone Modification Research Compound Library

621 compounds

A histone modification, a covalent post-translational modification (PTM) to histone proteins, includes methylation, phosphorylation, acetylation, ubiquitylation, and sumoylation, etc. In general, histone modifications are catalyzed by specific enzymes that act predominantly at the histone N-terminal tails involving amino acids such as lysine or arginine, as well as serine, threonine, tyrosine, etc. The PTMs made to histones can impact gene expression by altering chromatin structure or recruiting histone modifiers. Histone modifications act in diverse biological processes such as transcriptional activation/inactivation, chromosome packaging, and DNA damage/repair. Deregulation of histone modification contributes to many diseases, including cancer and autoimmune diseases.

MCE owns a unique collection of 621 bioactive compounds targeting Epigenetic Reader Domain, HDAC, Histone Acetyltransferase, Histone Demethylase, Histone Methyltransferase, Sirtuin, etc. Histone Modification Research Compound Library is a useful tool for histone modification research and drug screening.

Cat. No.	Product Name	Target	Research Area

HY-P2555

Histone H3 (23-34)	Peptides	Others
Histone H3 (23-34) is the histone H3 amino acid residues 23 to 34. Histone H3 (23-34) contains lysine residues at positions 23 and 27 that are subject to methylation and acetylation .

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