#	Aladdin ID	Assay Type	Description	Organism	Compounds	Reference	BAO Format	Source
1.	ALA3706041	B	Binding Assay: The method employed was adapted from the scientific literature and described in detail by Osbourn et al. (1993, Biochemistry, 32, 6229-6236). Recombinant human ERalpha and ERR proteins were purified from transfected Sf9-cells. The in vitro assays involved the use of either ERalpha or ERbeta proteins and [3H]E2, at a fixed concentration of 0.5 nM, as the labeled ligand. Recombinant human ERalpha or ERbeta proteins were dissolved in binding buffer (10 mM Tris-HCL, pH 7.5, 10% glycerol, 1 mM DTT, 1 mg/ml BSA) and duplicate aliquots were then incubated with [3H]E2 at a final concentration of 0.5 nM, together with a vehicle control (0.4% DMSO), or the same amount of vehicle containing increasing concentrations of unlabeled steroid ligands as competitors. After incubation for 2 h at 25 C., the unbound ligands were removed and the amounts of [3H]E2 bound to either ERalpha or ERbeta proteins were measured.	Homo sapiens	3	ALA3638825	cell-based format	BindingDB Database
2.	ALA3706107	B	Inhibition Assay: The method employed was adapted from the scientific literature and described in detail by Osboum et al. (1993, Biochemistry, 32, 6229-6236). Recombinant human ERalpha and ERbeta proteins were purified from transfected Sf9-cells. The in vitro assays involved the use of either ERalpha or ERbeta proteins and [3H]E2, at a fixed concentration of 0.5 nM, as the labeled ligand. Recombinant human ERalpha or ERbeta proteins were dissolved in binding buffer (10 mM Tris-HCL, pH 7.5, 10% glycerol, 1 mM DTT, 1 mg/ml BSA) and duplicate aliquots were then incubated with [3H]E2 at a final concentration of 0.5 nM, together with a vehicle control (0.4% DMSO), or the same amount of vehicle containing increasing concentrations of unlabeled steroid ligands as competitors. After incubation for 2 h at 25 C., the unbound ligands were removed and the amounts of [3H]E2 bound to either ERalpha or ERbeta proteins were measured.	Homo sapiens	3	ALA3638686	cell-based format	BindingDB Database
3.	ALA3707724	B	Inhibition Assay: The method employed was adapted from the scientific literature and described in detail by Osboum et al. (1993, Biochemistry, 32, 6229-6236). Recombinant human ERalpha and ERbeta proteins were purified from transfected Sf9-cells. The in vitro assays involved the use of either ERalpha or ERbeta proteins and [3H]E2, at a fixed concentration of 0.5 nM, as the labeled ligand. Recombinant human ERalpha or ERbeta proteins were dissolved in binding buffer (10 mM Tris-HCL, pH 7.5, 10% glycerol, 1 mM DTT, 1 mg/ml BSA) and duplicate aliquots were then incubated with [3H]E2 at a final concentration of 0.5 nM, together with a vehicle control (0.4% DMSO), or the same amount of vehicle containing increasing concentrations of unlabeled steroid ligands as competitors. After incubation for 2 h at 25 C., the unbound ligands were removed and the amounts of [3H]E2 bound to either ERalpha or ERbeta proteins were measured.	Homo sapiens	3	ALA3638686	cell-based format	BindingDB Database
4.	ALA3707687	B	Binding Assay: The method employed was adapted from the scientific literature and described in detail by Osbourn et al. (1993, Biochemistry, 32, 6229-6236). Recombinant human ERalpha and ERR proteins were purified from transfected Sf9-cells. The in vitro assays involved the use of either ERalpha or ERbeta proteins and [3H]E2, at a fixed concentration of 0.5 nM, as the labeled ligand. Recombinant human ERalpha or ERbeta proteins were dissolved in binding buffer (10 mM Tris-HCL, pH 7.5, 10% glycerol, 1 mM DTT, 1 mg/ml BSA) and duplicate aliquots were then incubated with [3H]E2 at a final concentration of 0.5 nM, together with a vehicle control (0.4% DMSO), or the same amount of vehicle containing increasing concentrations of unlabeled steroid ligands as competitors. After incubation for 2 h at 25 C., the unbound ligands were removed and the amounts of [3H]E2 bound to either ERalpha or ERbeta proteins were measured.	Homo sapiens	3	ALA3638825	cell-based format	BindingDB Database