Protein arginine methylation

By Targets:	Histone Methyltransferase (5)
By Research Areas:	Cancer (5)

Targets Recommended: Protein Arginine Deiminase SRPK

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-128717A

GSK3368715 dihydrochloride Maximum Cited Publications 11 Publications Verification EPZ019997 dihydrochloride	Histone Methyltransferase	Cancer
GSK3368715 dihydrochloride (EPZ019997 dihydrochloride) is an orally active, reversible, and S-adenosyl-L-methionine (SAM) uncompetitive *type I protein* arginine methyltransferases (PRMTs) inhibitor (IC₅₀*=3.1 nM (PRMT1), 48 nM (PRMT3), 1148 nM (PRMT4), 5.7 nM (PRMT6), 1.7 nM (PRMT8)). GSK3368715 dihydrochloride (EPZ019997 dihydrochloride) produces a shift in arginine* methylation states, alters exon usage, and has strong anti-cancer activity .

HY-Q36691

PRMT5-IN-30	Histone Methyltransferase	Cancer
PRMT5-IN-30 (compound 17) is a potent and selective protein arginine methyltransferase 5 (PRMT5) inhibitor with an IC₅₀ of 0.33 μM and a K_d of 0.987 μM. PRMT5-IN-30 exhibits a broad selectivity against a panel of other methyltransferases. PRMT5-IN-30 inhibits PRMT5 mediated SmD3 methylation .

HY-153421

PRMT5-IN-28	Histone Methyltransferase	Cancer
PRMT5-IN-28 (compound 36) is an inhibitor of protein arginine methyltransferase 5 (PRMT5) enzyme. Protein arginine methylation is a common post-translational modification involved in gene transcription, mRNA splicing, DNA repair, protein cellular localization, cell fate determination and signal transduction, etc. Abnormal PRMT5 can promote cancer cell proliferation, resist apoptosis, enhance invasion and metastasis, and affect immune escape .

HY-128717

GSK3368715 EPZ019997	Histone Methyltransferase	Cancer
GSK3368715 (EPZ019997) is an orally active, reversible, and S-adenosyl-L-methionine (SAM) uncompetitive *type I protein* arginine methyltransferases (PRMTs) inhibitor (IC₅₀*=3.1 nM (PRMT1), 48 nM (PRMT3), 1148 nM (PRMT4), 5.7 nM (PRMT6), 1.7 nM (PRMT8)). GSK3368715 (EPZ019997) produces a shift in arginine* methylation states, alters exon usage, and has strong anti-cancer activity .

HY-128717B

GSK3368715 trihydrochloride EPZ019997 trihydrochloride	Histone Methyltransferase	Cancer
GSK3368715 trihydrochloride (EPZ019997) is an orally active, reversible, and S-adenosyl-L-methionine (SAM) uncompetitive *type I protein* arginine methyltransferases (PRMTs) inhibitor (IC₅₀*=3.1 nM (PRMT1), 48 nM (PRMT3), 1148 nM (PRMT4), 5.7 nM (PRMT6), 1.7 nM (PRMT8)). GSK3368715 trihydrochloride (EPZ019997) produces a shift in arginine* methylation states, alters exon usage, and has strong anti-cancer activity .

Cat. No.	Product Name

HY-L024

Histone Modification Research Compound Library	629 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 629 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

629 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 629 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-P2556

Histone H3 (21-44)	Peptides	Others
Histone H3 (21-44), derived from histone H3 21-44 amino acids, is usually used as a substrate (such as protein arginine methyltransferases) for methylation assays .

MCE Japan Authorized Agent ナミキ商事株式会社コスモ・バイオ株式会社
Salutation			Country or Region *
Applicant Name *			Organization Name *
Department *
Email Address *			Product Name *
Cat. No.			Requested quantity *
Phone Number *
Remarks

Inhibitors & Agonists

Screening Libraries

Peptides

Name
Email *

	Sorry, but the email address you supplied was invalid.