ChEMBL ligand: CHEMBL443684 (A-855071.0, ABT-263, Navitoclax)
BCL2 apoptosis regulator/Apoptosis regulator Bcl-2 in Human [ChEMBL: CHEMBL4860] [GtoPdb: 2844] [UniProtKB: P10415] There should be some charts here, you may need to enable JavaScript!
Aspartyl/asparaginyl beta-hydroxylase in Human [ChEMBL: CHEMBL4680030] [UniProtKB: Q12797] There should be some charts here, you may need to enable JavaScript!
Bcl2-associated agonist of cell death in Human [ChEMBL: CHEMBL3817] [UniProtKB: Q92934] There should be some charts here, you may need to enable JavaScript!
Bcl-2-like 1/Bcl-2-like protein 1 in Human [ChEMBL: CHEMBL4625] [GtoPdb: 2845] [UniProtKB: Q07817] There should be some charts here, you may need to enable JavaScript!
Bcl-2-like 2/Bcl-2-like protein 2 in Human [ChEMBL: CHEMBL4677] [GtoPdb: 2846] [UniProtKB: Q92843] There should be some charts here, you may need to enable JavaScript!
CYP2C9/Cytochrome P450 2C9 in Human [ChEMBL: CHEMBL3397] [GtoPdb: 1326] [UniProtKB: P11712] There should be some charts here, you may need to enable JavaScript!
MCL1 apoptosis regulator, BCL2 family member/Induced myeloid leukemia cell differentiation protein Mcl-1 in Human [ChEMBL: CHEMBL4361] [GtoPdb: 2847] [UniProtKB: Q07820] There should be some charts here, you may need to enable JavaScript!

DB	Assay description	Assay Type	Standard value	Standard parameter	Original value	Original units	Original parameter	Reference
BCL2 apoptosis regulator/Apoptosis regulator Bcl-2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4860] [GtoPdb: 2844] [UniProtKB: P10415]
ChEMBL	Binding affinity to human full-length N-terminal His6-tagged prephosphorylated Bcl2 (2 to 206 residues) expressed in Escherichia coli S12 extract by isothermal titration calorimetry	B	5.74	pKd	1803	nM	Kd	J Med Chem (2020) 63: 13733-13744 [PMID:33197310]
ChEMBL	Binding Assay: Table 1: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was assessed using the Bcl2scan™ platform: T7 phage strains displaying BCL2 proteins were grown in parallel in 24-well blocks in an E. coli host derived from the BL21 strain. E. coli were grown to log-phase and infected with T7 phage from a frozen stock (multiplicity of infection=0.4) and incubated with shaking at 32° C. until lysis (90-150 minutes). The lysates were centrifuged (5,000×g) and filtered (0.2 μm) to remove cell debris. Streptavidin-coated magnetic beads were treated with biotinylated BIM peptide ligand for 30 minutes at room temperature to generate affinity resins for BCL2 assays. The liganded beads were blocked with excess biotin and washed with blocking buffer (SeaBlock (Pierce), 1% BSA, 0.05% Tween 20, 1 mM DTT) to remove unbound ligand and to reduce non-specific phage binding. Binding reactions were assembled by combining BCL2 proteins, liganded affinity beads, and test compounds in 1× binding buffer (20% SeaBlock, 0.17×PBS, 0.05% Tween 20, 6 mM DTT). Test compounds were prepared as 100× stocks in 100% DMSO. Kds were determined using an 11-point 3-fold compound dilution series with one DMSO control point. All compounds for Kd measurements were distributed by acoustic transfer in 100% DMSO. The compounds were then diluted directly into the assays such that the final concentration of DMSO was 0.9%. All reactions performed in polypropylene 384-well plates. Each was a final volume of 0.02 ml. The assay plates were incubated at room temperature with shaking for 1 hour and the affinity beads were washed with wash buffer (lx PBS, 0.05% Tween 20). The beads were then re-suspended in elution buffer (lx PBS, 0.05% Tween 20, 2 μM non-biotinylated affinity ligand) and incubated at room temperature with shaking for 30 minutes.	B	7.26	pKd	55	nM	Kd	US-11318134-B2. Benzamide compounds (2022)
ChEMBL	Binding Assay: Table 1: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was assessed using the Bcl2scan™ platform: T7 phage strains displaying BCL2 proteins were grown in parallel in 24-well blocks in an E. coli host derived from the BL21 strain. E. coli were grown to log-phase and infected with T7 phage from a frozen stock (multiplicity of infection=0.4) and incubated with shaking at 32° C. until lysis (90-150 minutes). The lysates were centrifuged (5,000×g) and filtered (0.2 μm) to remove cell debris. Streptavidin-coated magnetic beads were treated with biotinylated BIM peptide ligand for 30 minutes at room temperature to generate affinity resins for BCL2 assays. The liganded beads were blocked with excess biotin and washed with blocking buffer (SeaBlock (Pierce), 1% BSA, 0.05% Tween 20, 1 mM DTT) to remove unbound ligand and to reduce non-specific phage binding. Binding reactions were assembled by combining BCL2 proteins, liganded affinity beads, and test compounds in 1× binding buffer (20% SeaBlock, 0.17×PBS, 0.05% Tween 20, 6 mM DTT). Test compounds were prepared as 100× stocks in 100% DMSO. Kds were determined using an 11-point 3-fold compound dilution series with one DMSO control point. All compounds for Kd measurements were distributed by acoustic transfer in 100% DMSO. The compounds were then diluted directly into the assays such that the final concentration of DMSO was 0.9%. All reactions performed in polypropylene 384-well plates. Each was a final volume of 0.02 ml. The assay plates were incubated at room temperature with shaking for 1 hour and the affinity beads were washed with wash buffer (lx PBS, 0.05% Tween 20).	B	7.26	pKd	55	nM	Kd	US-11344546-B2. Benzamide compounds (2022)
ChEMBL	Bcl-2 Protein Family Binding Assay: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was assessed using the Bcl2scan™ platform: T7 phage strains displaying BCL2 proteins were grown in parallel in 24-well blocks in an E. coli host derived from the BL21 strain. E. coliwere grown to log-phase and infected with T7 phage from a frozen stock (multiplicity of infection=0.4) and incubated with shaking at 32° C. until lysis (90-150 minutes). The lysates were centrifuged (5,000×g) and filtered (0.2 μm) to remove cell debris. Streptavidin-coated magnetic beads were treated with biotinylated BIM peptide ligand for 30 minutes at room temperature to generate affinity resins for BCL2 assays. The liganded beads were blocked with excess biotin and washed with blocking buffer (SeaBlock (Pierce), 1% BSA, 0.05% Tween 20, 1 mM DTT) to remove unbound ligand and to reduce non-specific phage binding. Binding reactions were assembled by combining BCL2 proteins, liganded affinity beads, and test compounds in 1× binding buffer (20% SeaBlock, 0.17×PBS, 0.05% Tween 20, 6 mM DTT). Test compounds were prepared as 100× stocks in 100% DMSO. Kds were determined using an 11-point 3-fold compound dilution series with one DMSO control point. All compounds for Kd measurements were distributed by acoustic transfer in 100% DMSO. The compounds were then diluted directly into the assays such that the final concentration of DMSO was 0.9%. All reactions performed in polypropylene 384-well plates. Each was a final volume of 0.02 ml. The assay plates were incubated at room temperature with shaking for 1 hour and the affinity beads were washed with wash buffer (lx PBS, 0.05% Tween 20). The beads were then re-suspended in elution buffer (lx PBS, 0.05% Tween 20, 2 μM non-biotinylated affinity ligand) and incubated at room temperature with shaking for 30 minutes.	B	7.26	pKd	55	nM	Kd	US-11590126-B2. Benzamide compounds (2023)
ChEMBL	Binding affinity to human full-length N-terminal His6-tagged Bcl2 (2 to 206 residues) expressed in Escherichia coli S12 extract by isothermal titration calorimetry	B	7.69	pKd	20.6	nM	Kd	J Med Chem (2020) 63: 13733-13744 [PMID:33197310]
ChEMBL	Displacement of biotin-tagged MRPEPATIAQELRRIGDEFNA from C-terminal His-tagged human BCL-2 (1` to 211 residues) expressed in Escherichia coli measured after 2 hrs by AlphaScreen assay	B	9.19	pKd	0.65	nM	Kd	J Med Chem (2021) 64: 14230-14246 [PMID:34533954]
GtoPdb	-	-	9	pKi	<1	nM	Ki	J Med Chem (2008) 51: 6902-15 [PMID:18841882]
ChEMBL	Inhibition of Flu-Bax peptide binding to Bcl2 (unknown origin) by time-resolved fluorescence resonance energy transfer assay	B	9	pKi	<1	nM	Ki	Eur J Med Chem (2019) 177: 63-75 [PMID:31129454]
ChEMBL	Binding affinity to Bcl-2 (unknown origin) assessed as inhibition constant by competitive fluorescence polarization assay	B	9	pKi	<=1	nM	Ki	Eur J Med Chem (2020) 201: 112446-112446 [PMID:32563811]
ChEMBL	Binding affinity to human recombinant Bcl-2 assessed as inhibition constant by fluorescence polarization assay	B	9	pKi	<1	nM	Ki	J Med Chem (2024) 67: 5963-5998 [PMID:38597264]
ChEMBL	Inhibition of Bcl-2 (unknown origin) by fluorescence polarization assay	B	9	pKi	<1	nM	Ki	Eur J Med Chem (2018) 146: 471-482 [PMID:29407973]
ChEMBL	Binding affinity to Bcl-2 (unknown origin) by fluorescence polarization assay	B	9	pKi	<1	nM	Ki	Bioorg Med Chem Lett (2016) 26: 2105-2114 [PMID:26988306]
ChEMBL	Binding affinity to BCL2 (unknown origin) by fluorescence polarization assay	B	9	pKi	<1	nM	Ki	Medchemcomm (2016) 7: 778-787
ChEMBL	Displacement of fluorescein labeled Bax peptide from Bcl2 by fluorescence polarization assay	B	9	pKi	<1	nM	Ki	J Med Chem (2008) 51: 6902-6915 [PMID:18841882]
ChEMBL	Inhibition of BCL2 (unknown origin) by TR-FRET assay	B	9.3	pKi	<0.5	nM	Ki	J Med Chem (2020) 63: 11420-11435 [PMID:32539387]
ChEMBL	Binding affinity to Bcl-2 (unknown origin) assessed as dissociation constant incubated for 1 hrs by TR-FRET assay	B	10.36	pKi	0.04	nM	Ki	Sci Transl Med (2015) 7: null-null [PMID:25787766]
ChEMBL	Inhibition of Bcl2 (unknown origin)	B	10.36	pKi	0.04	nM	Ki	J Med Chem (2018) 61: 2636-2651 [PMID:28926247]
ChEMBL	Inhibition of Bcl2 (unknown origin)	B	10.36	pKi	0.04	nM	Ki	J Med Chem (2019) 62: 10005-10025 [PMID:31188592]
ChEMBL	Inhibition of BCL-2 (unknown origin) by fluorescence polarization assay	B	11	pKi	<0.01	nM	Ki	Eur J Med Chem (2019) 167: 76-95 [PMID:30769242]
ChEMBL	Inhibition of human BCL-2 overexpressed in mouse FDC-P1 cells assessed as cell viability after 24 hrs by Cell Titer Glo assay	B	7.82	pIC50	<15	nM	IC50	Bioorg Med Chem Lett (2014) 24: 3026-3033 [PMID:24881567]
ChEMBL	Displacement of Bax-derived peptide from Bcl-2 (unknown origin) by fluorescence polarization assay	B	7.99	pIC50	10.3	nM	IC50	Bioorg Med Chem (2018) 26: 443-454 [PMID:29229225]
ChEMBL	Inhibition of Bcl-2 (unknown origin) by fluorescence polarization assay	B	7.99	pIC50	10.3	nM	IC50	Eur J Med Chem (2023) 261: 115802-115802 [PMID:37713805]
ChEMBL	Homogeneous Time Resolved Fluorescence (HTRF) Assay: Table 2: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was also assessed using an HTRF assay. Background: FAM-Bak/Bad binds to surface pocket of the Bcl-2 protein family. This binding can be monitored by HTRF signals between anti-GST-Tb and FAM-peptide using GST-tagged Bcl proteins. Assay conditions: Bcl-2: 4 nM Bcl-2, 100 nM FAM-Bak peptide, Bcl-XL: 3 nM Bcl-XL, 40 nM FAM-Bad peptide in 20 mM K Phosphate, pH 7.5, 50 mM NaCl, 1 mM EDTA, 0.005% Triton X-100 and 1% DMSO (final). Assay procedure: Compounds were tested in 10-dose IC50 mode, in singlicate, with 3-fold serial dilution starting at 10 μM or 1 μM. Compound stock solutions were added to protein solution using Acoustic technology. The compounds were then incubated with protein for 10 min at room temperature. The respective FAM labeled peptide was added and incubated for another 10 min and then anti-GST-Tb was added. After 60 min at rt, the HTRF fluorescence signal ratio was measured.	B	8	pIC50	<10	nM	IC50	US-11318134-B2. Benzamide compounds (2022)
ChEMBL	Homogeneous Time Resolved Fluorescence (HTRF) Assay: Table 2: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was also assessed using an HTRF assay. Background: FAM-Bak/Bad binds to surface pocket of the Bcl-2 protein family. This binding can be monitored by HTRF signals between anti-GST-Tb and FAM-peptide using GST-tagged Bcl proteins. Assay conditions: Bcl-2: 4 nM Bcl-2, 100 nM FAM-Bak peptide, Bcl-XL: 3 nM Bcl-XL, 40 nM FAM-Bad peptide in 20 mM K Phosphate, pH 7.5, 50 mM NaCl, 1 mM EDTA, 0.005% Triton X-100 and 1% DMSO (final). Assay procedure: Compounds were tested in 10-dose IC50 mode, in singlicate, with 3-fold serial dilution starting at 10 μM or 1 μM. Compound stock solutions were added to protein solution using Acoustic technology.	B	8	pIC50	<10	nM	IC50	US-11344546-B2. Benzamide compounds (2022)
ChEMBL	Inhibition of recombinant human C-terminal 6xHis-tagged Bcl-2 (M1 to F212 residues) expressed in Escherichia coli using HyLite Fluor 647-labeled BIM peptide as substrate incubated for 120 to 180 mins by TR-FRET assay	B	8.7	pIC50	2	nM	IC50	Bioorg Med Chem Lett (2019) 29: 126682-126682 [PMID:31606346]
Aspartyl/asparaginyl beta-hydroxylase in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4680030] [UniProtKB: Q12797]
ChEMBL	Inhibition of N-His6-tagged human AspH (315-755) expressed in Escherichia coli BL21 (DE3) using 1 uM hFX-CP as substrate mixture with high 200 uM 2OG, 100 uM L-ascorbic acid and 2 uM FAS incubated for 35 mins by MS analysis	B	5.88	pIC50	1330	nM	IC50	Bioorg Med Chem (2020) 28: 115675-115675 [PMID:33069066]
ChEMBL	Inhibition of N-His6-tagged human AspH (315-755) expressed in Escherichia coli BL21 (DE3) using high 10 uM hFX-CP as substrate mixture with 10 uM 2OG, 100 uM L-ascorbic acid and 2 uM FAS incubated for 35 mins by MS analysis	B	5.92	pIC50	1210	nM	IC50	Bioorg Med Chem (2020) 28: 115675-115675 [PMID:33069066]
ChEMBL	Inhibition of N-His6-tagged human AspH (315-755) expressed in Escherichia coli BL21 (DE3) using 1 uM hFX-CP as substrate mixture with 3 uM 2OG, 100 uM L-ascorbic acid and 2 uM FAS incubated for 35 mins by MS analysis	B	5.99	pIC50	1030	nM	IC50	Bioorg Med Chem (2020) 28: 115675-115675 [PMID:33069066]
ChEMBL	Inhibition of N-His6-tagged human AspH (315-755) expressed in Escherichia coli BL21 (DE3) using 1 uM hFX-CP as substrate mixture with 3 uM 2OG, 100 uM L-ascorbic acid and high 20 uM FAS incubated for 35 mins by MS analysis	B	6.1	pIC50	800	nM	IC50	Bioorg Med Chem (2020) 28: 115675-115675 [PMID:33069066]
Bcl2-associated agonist of cell death in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3817] [UniProtKB: Q92934]
ChEMBL	Binding Assay: Table 1: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was assessed using the Bcl2scan™ platform: T7 phage strains displaying BCL2 proteins were grown in parallel in 24-well blocks in an E. coli host derived from the BL21 strain. E. coli were grown to log-phase and infected with T7 phage from a frozen stock (multiplicity of infection=0.4) and incubated with shaking at 32° C. until lysis (90-150 minutes). The lysates were centrifuged (5,000×g) and filtered (0.2 μm) to remove cell debris. Streptavidin-coated magnetic beads were treated with biotinylated BIM peptide ligand for 30 minutes at room temperature to generate affinity resins for BCL2 assays. The liganded beads were blocked with excess biotin and washed with blocking buffer (SeaBlock (Pierce), 1% BSA, 0.05% Tween 20, 1 mM DTT) to remove unbound ligand and to reduce non-specific phage binding. Binding reactions were assembled by combining BCL2 proteins, liganded affinity beads, and test compounds in 1× binding buffer (20% SeaBlock, 0.17×PBS, 0.05% Tween 20, 6 mM DTT). Test compounds were prepared as 100× stocks in 100% DMSO. Kds were determined using an 11-point 3-fold compound dilution series with one DMSO control point. All compounds for Kd measurements were distributed by acoustic transfer in 100% DMSO. The compounds were then diluted directly into the assays such that the final concentration of DMSO was 0.9%. All reactions performed in polypropylene 384-well plates. Each was a final volume of 0.02 ml. The assay plates were incubated at room temperature with shaking for 1 hour and the affinity beads were washed with wash buffer (lx PBS, 0.05% Tween 20).	B	7.26	pKd	55	nM	Kd	US-11344546-B2. Benzamide compounds (2022)
ChEMBL	Displacement of fluorescein labeled BAD peptide from Bcl-XL by fluorescence polarization assay	B	9	pKi	<1	nM	Ki	J Med Chem (2008) 51: 6902-6915 [PMID:18841882]
ChEMBL	Binding affinity to BH3 binding groove of BclXL	B	9.3	pKi	<0.5	nM	Ki	J Med Chem (2008) 51: 3661-3680 [PMID:18457385]
ChEMBL	Homogeneous Time Resolved Fluorescence (HTRF) Assay: Table 2: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was also assessed using an HTRF assay. Background: FAM-Bak/Bad binds to surface pocket of the Bcl-2 protein family. This binding can be monitored by HTRF signals between anti-GST-Tb and FAM-peptide using GST-tagged Bcl proteins. Assay conditions: Bcl-2: 4 nM Bcl-2, 100 nM FAM-Bak peptide, Bcl-XL: 3 nM Bcl-XL, 40 nM FAM-Bad peptide in 20 mM K Phosphate, pH 7.5, 50 mM NaCl, 1 mM EDTA, 0.005% Triton X-100 and 1% DMSO (final). Assay procedure: Compounds were tested in 10-dose IC50 mode, in singlicate, with 3-fold serial dilution starting at 10 μM or 1 μM. Compound stock solutions were added to protein solution using Acoustic technology.	B	8	pIC50	<10	nM	IC50	US-11344546-B2. Benzamide compounds (2022)
Bcl-2-like 1/Bcl-2-like protein 1 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4625] [GtoPdb: 2845] [UniProtKB: Q07817]
ChEMBL	Binding Assay: Table 1: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was assessed using the Bcl2scan™ platform: T7 phage strains displaying BCL2 proteins were grown in parallel in 24-well blocks in an E. coli host derived from the BL21 strain. E. coli were grown to log-phase and infected with T7 phage from a frozen stock (multiplicity of infection=0.4) and incubated with shaking at 32° C. until lysis (90-150 minutes). The lysates were centrifuged (5,000×g) and filtered (0.2 μm) to remove cell debris. Streptavidin-coated magnetic beads were treated with biotinylated BIM peptide ligand for 30 minutes at room temperature to generate affinity resins for BCL2 assays. The liganded beads were blocked with excess biotin and washed with blocking buffer (SeaBlock (Pierce), 1% BSA, 0.05% Tween 20, 1 mM DTT) to remove unbound ligand and to reduce non-specific phage binding. Binding reactions were assembled by combining BCL2 proteins, liganded affinity beads, and test compounds in 1× binding buffer (20% SeaBlock, 0.17×PBS, 0.05% Tween 20, 6 mM DTT). Test compounds were prepared as 100× stocks in 100% DMSO. Kds were determined using an 11-point 3-fold compound dilution series with one DMSO control point. All compounds for Kd measurements were distributed by acoustic transfer in 100% DMSO. The compounds were then diluted directly into the assays such that the final concentration of DMSO was 0.9%. All reactions performed in polypropylene 384-well plates. Each was a final volume of 0.02 ml. The assay plates were incubated at room temperature with shaking for 1 hour and the affinity beads were washed with wash buffer (lx PBS, 0.05% Tween 20). The beads were then re-suspended in elution buffer (lx PBS, 0.05% Tween 20, 2 μM non-biotinylated affinity ligand) and incubated at room temperature with shaking for 30 minutes.	B	7.26	pKd	55	nM	Kd	US-11318134-B2. Benzamide compounds (2022)
ChEMBL	Bcl-2 Protein Family Binding Assay: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was assessed using the Bcl2scan™ platform: T7 phage strains displaying BCL2 proteins were grown in parallel in 24-well blocks in an E. coli host derived from the BL21 strain. E. coliwere grown to log-phase and infected with T7 phage from a frozen stock (multiplicity of infection=0.4) and incubated with shaking at 32° C. until lysis (90-150 minutes). The lysates were centrifuged (5,000×g) and filtered (0.2 μm) to remove cell debris. Streptavidin-coated magnetic beads were treated with biotinylated BIM peptide ligand for 30 minutes at room temperature to generate affinity resins for BCL2 assays. The liganded beads were blocked with excess biotin and washed with blocking buffer (SeaBlock (Pierce), 1% BSA, 0.05% Tween 20, 1 mM DTT) to remove unbound ligand and to reduce non-specific phage binding. Binding reactions were assembled by combining BCL2 proteins, liganded affinity beads, and test compounds in 1× binding buffer (20% SeaBlock, 0.17×PBS, 0.05% Tween 20, 6 mM DTT). Test compounds were prepared as 100× stocks in 100% DMSO. Kds were determined using an 11-point 3-fold compound dilution series with one DMSO control point. All compounds for Kd measurements were distributed by acoustic transfer in 100% DMSO. The compounds were then diluted directly into the assays such that the final concentration of DMSO was 0.9%. All reactions performed in polypropylene 384-well plates. Each was a final volume of 0.02 ml. The assay plates were incubated at room temperature with shaking for 1 hour and the affinity beads were washed with wash buffer (lx PBS, 0.05% Tween 20). The beads were then re-suspended in elution buffer (lx PBS, 0.05% Tween 20, 2 μM non-biotinylated affinity ligand) and incubated at room temperature with shaking for 30 minutes.	B	7.26	pKd	55	nM	Kd	US-11590126-B2. Benzamide compounds (2023)
ChEMBL	Displacement of biotin-tagged LWAAQRYGRELRRMSDEFEGSFKGL from human BCL-XL expressed in Escherichia coli measured after 2 hrs by AlphaScreen assay	B	8.68	pKd	2.07	nM	Kd	J Med Chem (2021) 64: 14230-14246 [PMID:34533954]
ChEMBL	Inhibition of BCL-XL (unknown origin) by fluorescence polarization assay	B	7.32	pKi	48	nM	Ki	Eur J Med Chem (2019) 167: 76-95 [PMID:30769242]
ChEMBL	Binding affinity to Bcl-xl	B	7.44	pKi	36	nM	Ki	J Med Chem (2010) 53: 6779-6810 [PMID:20925433]
GtoPdb	-	-	9	pKi	<1	nM	Ki	J Med Chem (2008) 51: 6902-15 [PMID:18841882]
ChEMBL	Inhibition of Bcl-xL (unknown origin) by fluorescence polarization assay	B	9	pKi	<1	nM	Ki	Eur J Med Chem (2018) 146: 471-482 [PMID:29407973]
ChEMBL	Binding affinity to Bcl-xL by competitive fluorescence polarization assay	B	9	pKi	<1	nM	Ki	J Med Chem (2010) 53: 2577-2588 [PMID:20192224]
ChEMBL	Binding affinity to Bcl-XL (unknown origin) by fluorescence polarization assay	B	9	pKi	<1	nM	Ki	Bioorg Med Chem Lett (2016) 26: 2105-2114 [PMID:26988306]
ChEMBL	Binding affinity to His-tagged Bcl-xL (unknown origin) assessed as inhibition constant by competitive fluorescence polarization assay	B	9	pKi	<=1	nM	Ki	Eur J Med Chem (2020) 201: 112446-112446 [PMID:32563811]
ChEMBL	Binding affinity to Bcl-xL (unknown origin) assessed as inhibition constant	B	9	pKi	<1	nM	Ki	J Med Chem (2024) 67: 5963-5998 [PMID:38597264]
ChEMBL	Inhibition of Flu-Bax peptide binding to Bcl-xL (unknown origin) by time-resolved fluorescence resonance energy transfer assay	B	9.3	pKi	<0.5	nM	Ki	Eur J Med Chem (2019) 177: 63-75 [PMID:31129454]
ChEMBL	Binding affinity to Bcl-XL (unknown origin) by fluorescence polarization assay	B	9.3	pKi	<0.5	nM	Ki	Medchemcomm (2016) 7: 778-787
ChEMBL	Inhibition of F-Bak binding to GST-tagged BCL-XL (unknown origin) measured after 1 hr by TR-FRET assay	B	10	pKi	<0.1	nM	Ki	ACS Med Chem Lett (2021) 12: 1011-1016 [PMID:34141086]
ChEMBL	Binding affinity to Bcl-xl (unknown origin) assessed as dissociation constant incubated for 1 hrs by TR-FRET assay	B	10.26	pKi	0.06	nM	Ki	Sci Transl Med (2015) 7: null-null [PMID:25787766]
ChEMBL	Inhibition of Bcl-xL (unknown origin)	B	10.26	pKi	0.06	nM	Ki	J Med Chem (2018) 61: 2636-2651 [PMID:28926247]
ChEMBL	Inhibition of human BCL-xL overexpressed in mouse FDC-P1 cells assessed as cell viability after 24 hrs by Cell Titer Glo assay	B	7.22	pIC50	60	nM	IC50	Bioorg Med Chem Lett (2014) 24: 3026-3033 [PMID:24881567]
ChEMBL	Homogeneous Time Resolved Fluorescence (HTRF) Assay: Table 2: Binding to Bcl-2 proteins Bcl-2, and Bcl-XL was also assessed using an HTRF assay. Background: FAM-Bak/Bad binds to surface pocket of the Bcl-2 protein family. This binding can be monitored by HTRF signals between anti-GST-Tb and FAM-peptide using GST-tagged Bcl proteins. Assay conditions: Bcl-2: 4 nM Bcl-2, 100 nM FAM-Bak peptide, Bcl-XL: 3 nM Bcl-XL, 40 nM FAM-Bad peptide in 20 mM K Phosphate, pH 7.5, 50 mM NaCl, 1 mM EDTA, 0.005% Triton X-100 and 1% DMSO (final). Assay procedure: Compounds were tested in 10-dose IC50 mode, in singlicate, with 3-fold serial dilution starting at 10 μM or 1 μM. Compound stock solutions were added to protein solution using Acoustic technology. The compounds were then incubated with protein for 10 min at room temperature. The respective FAM labeled peptide was added and incubated for another 10 min and then anti-GST-Tb was added. After 60 min at rt, the HTRF fluorescence signal ratio was measured.	B	8	pIC50	<10	nM	IC50	US-11318134-B2. Benzamide compounds (2022)
ChEMBL	Inhibition of recombinant human N-terminal GST-tagged Bcl-xl (1 to 209 residues) expressed in Escherichia coli using HyLite Fluor 647-labeled BIM peptide as substrate incubated for 120 to 180 mins by TR-FRET assay	B	8.1	pIC50	<8	nM	IC50	Bioorg Med Chem Lett (2019) 29: 126682-126682 [PMID:31606346]
ChEMBL	Displacement of FITC-Bid from GST-tagged human Bcl-xL expressed in Escherichia coli after 2 hrs by TR-FRET assay	B	8.48	pIC50	3.3	nM	IC50	J Med Chem (2013) 56: 9635-9645 [PMID:24215352]
Bcl-2-like 2/Bcl-2-like protein 2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4677] [GtoPdb: 2846] [UniProtKB: Q92843]
ChEMBL	Inhibition of BCL-W (unknown origin) by fluorescence polarization assay	B	6.61	pKi	245	nM	Ki	Eur J Med Chem (2019) 167: 76-95 [PMID:30769242]
ChEMBL	Binding affinity to BCL-W (unknown origin) assessed as dissociation constant incubated for 1 hrs by TR-FRET assay	B	7.68	pKi	21	nM	Ki	Sci Transl Med (2015) 7: null-null [PMID:25787766]
ChEMBL	Binding affinity to Bcl-w (unknown origin) assessed as inhibition constant by competitive fluorescence polarization assay	B	9	pKi	<=1	nM	Ki	Eur J Med Chem (2020) 201: 112446-112446 [PMID:32563811]
ChEMBL	Inhibition of recombinant human N-terminal 6xHis-tagged Bcl-w (M1 to R171) expressed in Escherichia coli using HyLite Fluor 647-labeled Bim peptide as substrate incubated for 120 to 180 mins by TR-FRET assay	B	7.15	pIC50	70	nM	IC50	Bioorg Med Chem Lett (2019) 29: 126682-126682 [PMID:31606346]
CYP2C9/Cytochrome P450 2C9 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL3397] [GtoPdb: 1326] [UniProtKB: P11712]
ChEMBL	CYP 2C9 inhibition: The five isoform-selective probe substrate (in a cocktail manner) was used as a measure of activity for the individual cytochrome P450 (CYPs) in a pool of human liver microsomes, i.e., phenacetin for CYP1A2, diclofenac for CYP2C9, S-Mephenyloin for CYP2C19, dextromethorphan for CYP2D6, midazolam for CYP3A. Test compounds, at 7 concentration levels including zero, were incubated in human liver microsomes (HLM) together with the 5 probe substrate (in a cocktail manner). IC50 was determined by monitoring the reduction of the CYP activity as a function of test compound concentration and quantified by product formation using LC-MS/MS. Ketoconazole for CYP3A was included as quality control. All incubations were performed in singlet.	B	5.82	pIC50	1500	nM	IC50	US-11420968-B2. Bcl-2 inhibitors (2022)
MCL1 apoptosis regulator, BCL2 family member/Induced myeloid leukemia cell differentiation protein Mcl-1 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL4361] [GtoPdb: 2847] [UniProtKB: Q07820]
ChEMBL	Inhibition of Mcl-1 (unknown origin) by fluorescence polarization assay	B	6.26	pKi	550	nM	Ki	Eur J Med Chem (2018) 146: 471-482 [PMID:29407973]
ChEMBL	Inhibition of F-Bak binding to GST-tagged MCL1 (unknown origin) measured after 1 hr by TR-FRET assay	B	6.65	pKi	>224	nM	Ki	ACS Med Chem Lett (2021) 12: 1011-1016 [PMID:34141086]
ChEMBL	Binding affinity to MCL-1 (unknown origin) assessed as dissociation constant incubated for 1 hrs by TR-FRET assay	B	6.65	pKi	>224	nM	Ki	Sci Transl Med (2015) 7: null-null [PMID:25787766]
ChEMBL	Inhibition of Flu-Bax peptide binding to MCl-1 (unknown origin) by time-resolved fluorescence resonance energy transfer assay	B	9	pKi	<1	nM	Ki	Eur J Med Chem (2019) 177: 63-75 [PMID:31129454]
ChEMBL	Displacement of FITC-Bid from GST-tagged human Mcl-1 expressed in Escherichia coli after 2 hrs by TR-FRET assay	B	4.52	pIC50	>30000	nM	IC50	J Med Chem (2013) 56: 9635-9645 [PMID:24215352]
ChEMBL	Inhibition of recombinant human C-terminal 6xHis-tagged Mcl-1 (E171 ti G327) expressed in Escherichia coli using biotin-labeled BIM peptide as substrate incubated for 120 to 180 mins by TR-FRET assay	B	5	pIC50	>10000	nM	IC50	Bioorg Med Chem Lett (2019) 29: 126682-126682 [PMID:31606346]
ChEMBL	Binding affinity to MCL1 (unknown origin) by fluorescence polarization assay	B	6.3	pIC50	500	nM	IC50	Medchemcomm (2016) 7: 778-787

ChEMBL data shown on this page come from version 36:

Zdrazil B, Felix E, Hunter F, Manners EJ, Blackshaw J, Corbett S, de Veij M, Ioannidis H, Lopez DM, Mosquera JF, Magarinos MP, Bosc N, Arcila R, Kizilören T, Gaulton A, Bento AP, Adasme MF, Monecke P, Landrum GA, Leach AR. (2024). The ChEMBL Database in 2023: a drug discovery platform spanning multiple bioactivity data types and time periods. Nucleic Acids Res., 52(D1). DOI: 10.1093/nar/gkad1004. [EPMCID:10767899] [PMID:37933841]
Davies M, Nowotka M, Papadatos G, Dedman N, Gaulton A, Atkinson F, Bellis L, Overington JP. (2015) 'ChEMBL web services: streamlining access to drug discovery data and utilities.' Nucleic Acids Res., 43(W1). DOI: 10.1093/nar/gkv352. [EPMCID:25883136]