| Identification | Back Directory | [Name]
XY1 | [CAS]
1624117-53-8 | [Synonyms]
XY1
CS-2431
XY1 NEW
XY1; XY 1
XY1;XY-1;XY 1
XY-1 (Negative of SGC-707)
N-2-Naphthalenyl-N'-[2-oxo-2-(1-pyrrolidinyl)ethyl]urea
Urea, N-2-naphthalenyl-N'-[2-oxo-2-(1-pyrrolidinyl)ethyl]-
1-(naphthalen-2-yl)-3-[2-oxo-2-(pyrrolidin-1-yl)ethyl]urea | [Molecular Formula]
C17H19N3O2 | [MDL Number]
MFCD28397755 | [MOL File]
1624117-53-8.mol | [Molecular Weight]
297.35 |
| Chemical Properties | Back Directory | [Boiling point ]
514.8±42.0 °C(Predicted) | [density ]
1.284±0.06 g/cm3(Predicted) | [storage temp. ]
Sealed in dry,Store in freezer, under -20°C | [solubility ]
DMF: 10 mg/ml; DMSO: 25 mg/ml; DMSO:PBS (pH 7.2) (1:1): 0.5 mg/ml | [form ]
A crystalline solid | [pka]
12.62±0.46(Predicted) | [color ]
White to off-white |
| Hazard Information | Back Directory | [Description]
Protein arginine N-methyltransferase 3 (PRMT3, ) is a predominantly cytoplasmic enzyme that is constitutively expressed. SGC707 is a potent, selective allosteric inhibitor of PRMT3 (IC50 = 50 nM). It inhibits the methylation of histones in cells with an IC50 value below 1 μM. XY1 is a close analog of SGC707 that is completely inactive against PRMT3 at concentrations as high as 100 μM. It is intended to be used as a negative control for SGC707 in studies involving PRMT3 action. See the Structural Genomics Consortium (SGC) website for more information. | [Uses]
XY1 acts as a close analog of SGC707 that is completely inactive against PRMT3, inhibiting the methylation of histones in cells. | [storage]
Store at -20°C | [References]
[1] J TANG. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation.[J]. The Journal of Biological Chemistry, 1998, 273 27: 16935-16945. DOI: 10.1074/jbc.273.27.16935
[2] WOLF S S. The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans.[J]. Cellular and Molecular Life Sciences, 2009, 66 13: 2109-2121. DOI: 10.1007/s00018-009-0010-x
[3] DR. H. üMIT KANISKAN. A Potent, Selective and Cell-Active Allosteric Inhibitor of Protein Arginine Methyltransferase 3 (PRMT3)?[J]. Angewandte Chemie International Edition, 2015, 54 17: 5166-5170. DOI: 10.1002/anie.201412154 |
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