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Found 11 Enz. Inhib. hit(s) with Target = 'Histone-lysine N-methyltransferase EHMT2' and Ligand = 'BDBM50315537'
TargetHistone-lysine N-methyltransferase EHMT2(Homo sapiens (Human))
Riken Advanced Science Institute

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.40E+3nMAssay Description:Inhibition of protein lysine methyltransferase G9a (unknown origin) by ELISA assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Homo sapiens (Human))
Riken Advanced Science Institute

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.40E+3nMAssay Description:Inhibition of GST-tagged G9a after 1 hr by radioactive filter-binding assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Mus musculus)
TBA

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.50E+3nMAssay Description:Inhibition of mouse G9aMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Homo sapiens (Human))
Riken Advanced Science Institute

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.50E+3nMAssay Description:Inhibition of G9a (unknown origin) using SAM/biotinylated H3 as substrate preincubated for 1 hr followed by substrate addition measured after 2 hrs b...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Mus musculus)
TBA

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.50E+3nMAssay Description:Inhibition of mouse Histone-lysine N-methyltransferase G9aMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Homo sapiens (Human))
Riken Advanced Science Institute

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.50E+3nMAssay Description:Inhibition human G9a catalytic domainMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Mus musculus)
TBA

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.50E+3nMAssay Description:Inhibition of mouse G9aMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Homo sapiens (Human))
Riken Advanced Science Institute

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.50E+3nMAssay Description:Inhibition of GST-tagged EHMT2 (unknown origin) using biotinylated-H3 peptide as substrate preincubated for 1 hr followed by substrate addition and m...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Homo sapiens (Human))
Riken Advanced Science Institute

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.57E+3nMAssay Description:Inhibition of N-terminal GST-tagged recombinant human Histone-lysine N-methyltransferase G9a using S-(5'-adenosyl)-L-methionine chloride as substrate...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Homo sapiens (Human))
Riken Advanced Science Institute

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  2.60E+3nMAssay Description:Inhibition of N-terminal GST-tagged recombinant human Histone-lysine N-methyltransferase G9a using S-(5'-adenosyl)-L-methionine chloride as substrate...More data for this Ligand-Target Pair
In DepthDetails ArticlePubMed
TargetHistone-lysine N-methyltransferase EHMT2(Homo sapiens (Human))
Riken Advanced Science Institute

Curated by ChEMBL
LigandPNGBDBM50315537(CHEMBL1089316 | chaetocin)
Affinity DataIC50:  7.20E+3nMAssay Description:Inhibition of protein lysine methyltransferase G9a (unknown origin) by modified ELISA assayMore data for this Ligand-Target Pair
In DepthDetails ArticlePubMed