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MS049

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Chemical Structure| 1502816-23-0 同义名 : -
CAS号 : 1502816-23-0
货号 : A567534
分子式 : C15H24N2O
纯度 : 98%+
分子量 : 248.364
MDL号 : MFCD30489737
存储条件：

粉末 Keep in dark place,Sealed in dry,Room Temperature

液体 -20°C:3-6个月-80°C:12个月
溶解度 :

DMSO: 30 mg/mL(120.79 mM)，注意：DMSO长时间开封后，会吸水并导致溶解能力下降，请避免使用长期开封的DMSO

H2O: 100 mg/mL(402.64 mM)
动物实验配方：
生物活性
描述 Histone arginine methylation is a key post-translational modification that mediates epigenetic events that activate or repress gene transcription. Protein arginine methyltransferases (PRMTs) are the driving force for the process of arginine methylation, and the core histone proteins have been shown to be substrates for most PRMT family members[2].MS049 is a potent, selective, and cell-active dual inhibitor of PRMT4 and PRMT6 with IC50s of 34 nM and 43 nM, respectively. MS049 reduces levels of Med12me2a and H3R2me2a in HEK293 cells. MS049 is not toxic and does not affect the growth of HEK293 cells. MS049 (0.1-10 μM; 20 hours) reduces the H3R2me2a mark in HEK293 cells in a concentration dependent manner (IC50=0.97±0.05 μM).MS049 (0.1-100 μM; 72 hours) inhibits endogenous PRMT4 methyltransferase activity in a concentration dependent manner resulting in reduced levels of cellular asymmetric arginine dimethylation of Med12 (Med12-Rme2a, IC50=1.4±0.1 μM) in HEK293 cells.MS049 is selective for PRMT4 and PRMT6 over a broad range of epigenetic modifiers, including other PRMTs, PKMTs, DNMTs, KDMs, and methyllysine/methylarginine reader proteins, and non-epigenetic targets[3].
实验方案
1mg 5mg 10mg

1 mM

5 mM

10 mM

4.03mL

0.81mL

0.40mL

20.13mL

4.03mL

2.01mL

40.26mL

8.05mL

4.03mL
参考文献

[1]Shen Y, Szewczyk MM, et al. Discovery of a Potent, Selective, and Cell-Active Dual Inhibitor of Protein Arginine Methyltransferase 4 and Protein Arginine Methyltransferase 6. J Med Chem. 2016 Oct 13;59(19):9124-9139.

[2] Melody D Fulton, Mengtong Cao,et al. The macromolecular complexes of histones affect protein arginine methyltransferase activities. J Biol Chem. 2021 Oct;297(4):101123.

[3] Shen Y et al. Discovery of a Potent, Selective, and Cell-Active Dual Inhibitor of Protein Arginine Methyltransferase 4 and Protein Arginine Methyltransferase 6. J Med Chem. 2016 Sep 15.