iDeg-6

iDeg-6 potently inhibits kynurenine formation in IFN-γ-stimulated BxPC3 cells with an IC₅₀ of 16 nM^[1].
iDeg-6 (0.5-10000 nM; 24 h) dose-dependently depletes IDO1 protein in IFN-γ-pretreated, washout BxPC3 cells with a DC₅₀ of 6.5 nM and a D_max of 70% at 100 nM^[1].
iDeg-6 (0.01-10 µM; 24 h) dose-dependently depletes IDO1 protein in SKOV-3 cells over 24 h of incubation^[1].
iDeg-6 (0.01-1 µM; 24 h) dose-dependently depletes IDO1 protein in BT549 cells over 24 h of incubation^[1].
iDeg-6 (1-100 nM; 24 h) mediated IDO1 protein depletion in IFN-γ-pretreated, washout wildtype U2OS cells is dependent on KLHDC3, as knockout of KLHDC3 abolishes the degradation and elevates baseline IDO1 levels^[1].
iDeg-6 (10^-3-10⁵ nM) mediated IDO1 depletion in KBM7-BFP-IDO1 cells is dependent on KLHDC3, as knockout of KLHDC3 abolishes the degradation and elevates baseline IDO1 levels^[1].
iDeg-6 (10-10000 nM)-bound full-length IDO1 binds to CRL2^KLHDC3 with similar high affinity as apo-IDO1, with an IC₅₀ of 118 nM in a competitive ubiquitination assay^[1].
iDeg-6 potently inhibits recombinant human IDO1 enzymatic activity in vitro with an IC₅₀ of 1.6 µM^[1].
iDeg-6 (48 h) potently inhibits IDO1 enzymatic activity in IFN-γ-stimulated BxPC3 cells with an IC₅₀ of 16 nM^[2].
iDeg-6 (0.5-10000 nM; 24 h) dose-dependently depletes IDO1 protein in IFN-γ-pretreated BxPC3 cells with a DC₅₀ of 6.5 nM and a D_max of 70% at 100 nM^[2].
iDeg-6 (0.01-1 μM; 24 h) dose-dependently depletes IDO1 protein in BT549 cells after 24 h of treatment^[2].
iDeg-6 (1-100 nM; 24 h) dose-dependently depletes IDO1 protein in IFN-γ-pretreated wild-type U2OS cells after 24 h of treatment, and this degradation is dependent on the E3 ligase KLHDC3^[2].
iDeg-6 (90 min) potently inhibits in vitro IDO1 enzymatic activity with an IC₅₀ of 1.6 μM^[2].
iDeg-6 (50 μM; 3 h) stabilizes recombinant human IDO1 protein in vitro, as measured by nanoDSF, more effectively than iDeg-1, iDeg-2, and iDeg-3^[2].
iDeg-6 (100 μM; 3 h) displaces haem from recombinant human holo-IDO1 in vitro, as measured by UV-vis spectroscopy, more effectively than iDeg-1, iDeg-2, and iDeg-3^[2].
iDeg-6 (14 nM; 48 h) inhibits kynurenine production in BxPC3 cells with an IC₅₀ of 14 nM^[3].
iDeg-6 (14 μM; 45 min) shows weak inhibition of recombinant human IDO1 enzymatic activity, with 40% inhibition at 14 μM and an IC₅₀ >14 μM^[3].
iDeg-6 (6.5-100 nM; 24 h) potently degrades IDO1 protein in IFN-γ-stimulated cells with a DC₅₀ of 6.5 nM and 74% maximum degradation at 100 nM^[3].
iDeg-6 (25 μM) binds to recombinant human IDO1 with a K_d of 1.46 μM in an enthalpy-driven interaction^[3].
iDeg-6 (1 μM; 24 h (pre-conditioning)) reduces the migratory capacity of SKOV-3 cells by depleting IDO1, targeting its non-enzymatic protumorigenic function^[2].
iDeg-6 (10 μM; 4 h) selectively reduces IDO1 protein levels in SKOV-3 cells, with no other targeted protein degradation detected among 4607 analyzed proteins^[3].
iDeg-6 (6.5-16 nM; 100 nM) potently inhibits IDO1 activity in BxPC3 cells with an IC₅₀ of 16 nM and induces IDO1 protein degradation with a DC₅₀ of 6.5 nM and 70% maximum degradation at 100 nM via recruitment of the KLHDC3 E3 ligase^[4].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.