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Results for "

posttranslational modification (PTM)

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Biochemical Assay Reagents (1) Endogenous Metabolite (1)
By Research Areas:	Cancer (2) Cardiovascular Disease (1) Inflammation/Immunology (1) Metabolic Disease (1)

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Screening Libraries

Biochemical Assay Reagents

Peptides

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-126171

Hypusine	Endogenous Metabolite	Others
Hypusine is a natural amino acid. The post-translational synthesis of hypusine is mainly catalyzed by deoxyhypusine synthase (DHPS) and deoxyhypusine hydroxylase (DOHH) .

Cat. No.	Product Name

HY-L024

Histone Modification Research Compound Library	670 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 670 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

670 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 670 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.

HY-L915

Lysine Focused Covalent Fragment Library	445 compounds
Lysine is the second most common target residue used in the design of TCIs and related covalent ligands. Its appeal lies in its abundance in human proteins, which is approximately three times higher than that of cysteine (5.8% vs. 1.9%). This significantly increases the number of proteins suitable for covalent targeting, especially given that many human proteins lack ligandable cysteine residues. Moreover, it has been suggested that functional lysines have a lower probability of being replaced by mutation, as they often play a crucial role in catalysis by acting as bases or nucleophiles. Additionally, lysines are essential for maintaining the structural integrity of proteins and for regulating post-translational modifications (PTMs). Consequently, targeting lysine has garnered significant interest in recent years. Through careful selection, we constructed a structural filter containing over 110 electrophilic groups. By analyzing the electrophilic fragments selected by the structural filter, we removed any molecules with trivial or undesirable structural features. Ultimately, we obtained 445 fragment molecules which can target lysine residue and can be used for fragment-based covalent drug discovery.

Lysine Focused Covalent Fragment Library

445 compounds

Lysine is the second most common target residue used in the design of TCIs and related covalent ligands. Its appeal lies in its abundance in human proteins, which is approximately three times higher than that of cysteine (5.8% vs. 1.9%). This significantly increases the number of proteins suitable for covalent targeting, especially given that many human proteins lack ligandable cysteine residues. Moreover, it has been suggested that functional lysines have a lower probability of being replaced by mutation, as they often play a crucial role in catalysis by acting as bases or nucleophiles. Additionally, lysines are essential for maintaining the structural integrity of proteins and for regulating post-translational modifications (PTMs). Consequently, targeting lysine has garnered significant interest in recent years.

Through careful selection, we constructed a structural filter containing over 110 electrophilic groups. By analyzing the electrophilic fragments selected by the structural filter, we removed any molecules with trivial or undesirable structural features. Ultimately, we obtained 445 fragment molecules which can target lysine residue and can be used for fragment-based covalent drug discovery.

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-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 .

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 .

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