OG-L002 Chemical Properties

Boiling point:

416.7±45.0 °C(Predicted)

Density 

1.193±0.06 g/cm3(Predicted)

storage temp. 

Store at -20°C

solubility 

insoluble in H2O; ≥22.5 mg/mL in DMSO; ≥6.82 mg/mL in EtOH

form 

solid

pka

9.78±0.10(Predicted)

color 

White to yellow

OG-L002 Usage And Synthesis

Description

Lysine-specific demethylase 1 (LSD1) is a protein lysine demethylase that specifically demethylates histone H3 lysine 4 (H3K4) and H3K9, resulting in transcriptional repression. Host LSD1 is also recruited by certain viruses to limit H3K9 methylation, which can repress viral genes necessary for infection. Lysine-specific demethylase 1 (LSD1) is a protein lysine demethylase that specifically demethylates histone H3 lysine 4 (H3K4) and H3K9, resulting in transcriptional repression. Host LSD1 is also recruited by certain viruses to limit H3K9 methylation, which can repress viral genes necessary for infection. OG-L002 is a potent inhibitor of LSD1 (IC₅₀ = 0.02 μM) that less effectively inhibits the monoamine oxidases A (MAO-A) and MAO-B (IC₅₀s = 1.38 and 0.72 μM). It blocks the expression of immediate early (IE) genes of herpes simplex virus (HSV) in HeLa cells but not that of cellular control genes. OG-L002 also reduces the expression of human cytomegalovirus IE genes and adenovirus E1A gene in mammalian cells. It is effective in vivo, repressing HSV primary infection in mice and blocking HSV reactivation from latency in a mouse ganglion explant model.

Uses

OG-L002 is a novel, potent, and selective LSD1/KDM1A inhibitor that epigenetically blocks the herpes simplex lytic replication and reactivation from latency.

in vivo

target

LSD1

storage

Store at -20°C

References

[1] FEDERICO FORNERIS. Human histone demethylase LSD1 reads the histone code.[J]. The Journal of Biological Chemistry, 2005, 280 50: 41360-41365. DOI: 10.1074/jbc.m509549200
[2] YU LIANG. A novel selective LSD1/KDM1A inhibitor epigenetically blocks herpes simplex virus lytic replication and reactivation from latency.[J]. mBio, 2013, 4 1: e00558-12. DOI: 10.1128/mbio.00558-12

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