post-translational modifications (PTMs)

By Targets:	Biochemical Assay Reagents (1) HDAC (1)
By Research Areas:	Cancer (3) Cardiovascular Disease (1) Inflammation/Immunology (1) Metabolic Disease (1)

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-W286743

Nε-(Carboxymethyl)-L-lysine CML; N6-(Carboxymethyl)-L-lysine; Nε-(1-Carboxymethyl)-L-lysine	Biochemical Assay Reagents	Cardiovascular Disease Metabolic Disease Cancer
Nε-(Carboxymethyl)-L-lysine (CML) is a unique post-translational modification (PTM) of proteins that is generated by the non-enzymatic glycation of lysine residues. Nε-(Carboxymethyl)-L-lysine is a relatively recently discovered modification, and has been found to be a major component of the advanced glycation endproducts (AGEs) found in multiple human diseases, such as diabetes, Alzheimer’s disease, and cancer .

HY-151364

HDAC6/8/BRPF1-IN-1	HDAC	Cancer
HDAC6/8/BRPF1-IN-1 is a dual inhibitor of both HDAC6/8 and the bromodomain and PHD finger containing protein 1 (BRPF1). HDAC6/8/BRPF1-IN-1 has inhibitory activity for HDAC1, HDAC6 and HDAC8 with IC₅₀ values of 797 nM, 344 nM and 908 nM, respectively. HDAC6/8/BRPF1-IN-1 has inhibitory activity for BRPF1 with an K_d value of 175.2 nM. HDAC6/8/BRPF1-IN-1 can be used for the research of cancer .

Cat. No.	Product Name

HY-L024

Histone Modification Research Compound Library	636 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 636 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

636 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 636 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	Type

HY-W286743

Nε-(Carboxymethyl)-L-lysine CML; N6-(Carboxymethyl)-L-lysine; Nε-(1-Carboxymethyl)-L-lysine	Biochemical Assay Reagents
Nε-(Carboxymethyl)-L-lysine (CML) is a unique post-translational modification (PTM) of proteins that is generated by the non-enzymatic glycation of lysine residues. Nε-(Carboxymethyl)-L-lysine is a relatively recently discovered modification, and has been found to be a major component of the advanced glycation endproducts (AGEs) found in multiple human diseases, such as diabetes, Alzheimer’s disease, and cancer .

Nε-(Carboxymethyl)-L-lysine

CML; N6-(Carboxymethyl)-L-lysine; Nε-(1-Carboxymethyl)-L-lysine

Biochemical Assay Reagents

Nε-(Carboxymethyl)-L-lysine (CML) is a unique post-translational modification (PTM) of proteins that is generated by the non-enzymatic glycation of lysine residues. Nε-(Carboxymethyl)-L-lysine is a relatively recently discovered modification, and has been found to be a major component of the advanced glycation endproducts (AGEs) found in multiple human diseases, such as diabetes, Alzheimer’s disease, and cancer .

Cat. No.	Product Name	Target	Research Area

HY-P10111A

Histone H3K9me3 (1-15) (TFA) H3(1-15)K9me3 TFA	Peptides	Others
Histone H3K9me3 (1-15) (H3(1-15)K9me3) TFA is used as substrate. Histone H3K9me3 is a histone posttranslational modification (PTM) that has emerged as hallmark of pericentromeric heterochromatin .

HY-P10111

Histone H3K9me3 (1-15) H3(1-15)K9me3	Peptides	Inflammation/Immunology Cancer
Histone H3K9me3 (1-15) (H3(1-15)K9me3) is a histone posttranslational modification (PTM) that has emerged as hallmark of pericentromeric heterochromatin. Trimethylation of histone H3 at lysine 9 is associated with gene repression, prevents transcription factor binding .

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