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Pathways Recommended:	Epigenetics

Results for "

epigenetic modification

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Endogenous Metabolite (4) Histone Methyltransferase (3)
By Research Areas:	Cancer (3)

Inhibitors & Agonists

Screening Libraries

Peptides

Natural
Products

Isotope-Labeled Compounds

Targets Recommended: Epigenetic Reader Domain

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-I0626

Cytosine 1 Publications Verification	Endogenous Metabolite	Others
Cytosine is one of the four main bases found in DNA and RNA. Cytosine modifications exhibit circadian oscillations that are involved in epigenetic diversity and aging .

HY-144187

PRMT5-IN-16	Histone Methyltransferase	Cancer
PRMT5-IN-16 (Compound 20) is a PRMT5 inhibitor with anti-tumor activity. PRMT5 is a type of protein arginine methyltransferase, and is a new anti-tumor target related to epigenetic modification .

HY-144188

PRMT5-IN-17	Histone Methyltransferase	Cancer
PRMT5-IN-17 (Compound 6) is a PRMT5 inhibitor with anti-tumor activity. PRMT5 is a type of protein arginine methyltransferase, and is a new anti-tumor target related to epigenetic modification .

HY-I0626S2

Cytosine-d2	Endogenous Metabolite	Others
Cytosine-d₂ is the deuterium labeled Cytosine[1]. Cytosine is one of the four main bases found in DNA and RNA. Cytosine modifications exhibit circadian oscillations that are involved in epigenetic diversity and aging[2][3].

HY-P3822

PRMT5-IN-23	Histone Methyltransferase	Cancer
PRMT5-IN-23 (compound 50) is an inhibitor of protein arginine methyltransferase 5 (PRMT5) with anti-tumor activity. PRMT5 is a type of protein arginine methyltransferase, and is a new anti-tumor target related to epigenetic modification .

HY-I0626S1

Cytosine-13C,15N2	Endogenous Metabolite	Others
Cytosine- ¹³C, ¹⁵N₂ is the ¹³C and ¹⁵N labeled Cytosine[1]. Cytosine is one of the four main bases found in DNA and RNA. Cytosine modifications exhibit circadian oscillations that are involved in epigenetic diversity and aging[2][3].

HY-I0626S

Cytosine-2,4-13C2-1,3-15N2	Endogenous Metabolite	Others
Cytosine- ¹³C₂, ¹⁵N₂ is the ¹³C-labeled and ¹⁵N-labeled Cytosine. Cytosine is one of the four main bases found in DNA and RNA. Cytosine modifications exhibit circadian oscillations that are involved in epigenetic diversity and aging[1][2].

Cat. No.	Product Name

HY-L024

Histone Modification Research Compound Library	614 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 614 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

614 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 614 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-L005

Epigenetics Compound Library	1225 compounds
Epigenetics refers to changes in phenotype that are not rooted in DNA sequence. Many types of epigenetic processes have been identified, including DNA methylation, alteration in the structure of histone proteins and gene regulation by small noncoding microRNAs. Modification of DNA, protein, or RNA, resulting in changes to the function and/or regulation of these molecules, without altering their primary sequences, reveals the complexities of cellular differentiation, embryology, the regulation of gene expression, aging, cancer, and other diseases. MCE provide a unique collection of 1225 epigenetics-related compounds that can be used in the research of the related diseases.

Epigenetics Compound Library

1225 compounds

Epigenetics refers to changes in phenotype that are not rooted in DNA sequence. Many types of epigenetic processes have been identified, including DNA methylation, alteration in the structure of histone proteins and gene regulation by small noncoding microRNAs. Modification of DNA, protein, or RNA, resulting in changes to the function and/or regulation of these molecules, without altering their primary sequences, reveals the complexities of cellular differentiation, embryology, the regulation of gene expression, aging, cancer, and other diseases.

MCE provide a unique collection of 1225 epigenetics-related compounds that can be used in the research of the related diseases.

HY-L169

Anti-Drug-Resistant Compound Library	325 compounds
Resistance refers to the decrease in the effectiveness of drugs in treating diseases or symptoms. Due to the increasing global antibiotic resistance, it may threaten our ability to treat common infectious diseases. Drug resistance is also the main cause of chemotherapy failure in malignant tumors. In approximately 50% of cases, drug resistance exists even before chemotherapy begins. There are many mechanisms of anticancer drug resistance, including increased protein expression that leads to drug removal, mutations in drug binding sites, recovery of tumor protein production, and pre-existing genetic heterogeneity in tumor cell populations. In addition, the issue of drug resistance seems to have affected the development of new anticancer drugs. Drug resistance may be caused by various conditions, such as mutations, epigenetic modifications, and upregulation of drug efflux protein expression. Overcoming multidrug resistance in cancer treatment is becoming increasingly important. MCE designs a unique collection of 325 anti-drug-resistant compounds. It is a good tool to be used for research on cancer and other diseases.

Anti-Drug-Resistant Compound Library

325 compounds

Resistance refers to the decrease in the effectiveness of drugs in treating diseases or symptoms. Due to the increasing global antibiotic resistance, it may threaten our ability to treat common infectious diseases. Drug resistance is also the main cause of chemotherapy failure in malignant tumors. In approximately 50% of cases, drug resistance exists even before chemotherapy begins. There are many mechanisms of anticancer drug resistance, including increased protein expression that leads to drug removal, mutations in drug binding sites, recovery of tumor protein production, and pre-existing genetic heterogeneity in tumor cell populations. In addition, the issue of drug resistance seems to have affected the development of new anticancer drugs. Drug resistance may be caused by various conditions, such as mutations, epigenetic modifications, and upregulation of drug efflux protein expression. Overcoming multidrug resistance in cancer treatment is becoming increasingly important.

MCE designs a unique collection of 325 anti-drug-resistant compounds. It is a good tool to be used for research on cancer and other diseases.

PRMT5-IN-23	Histone Methyltransferase	Cancer
PRMT5-IN-23 (compound 50) is an inhibitor of protein arginine methyltransferase 5 (PRMT5) with anti-tumor activity. PRMT5 is a type of protein arginine methyltransferase, and is a new anti-tumor target related to epigenetic modification .

Cat. No.	Product Name	Category	Target	Chemical Structure