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Merck
CN

SML3043

XL188

≥98% (HPLC)

别名:

((R)-N-(3-((4-hydroxy-1-(3-phenylbutanoyl)piperidin-4-yl)methyl)-4-oxo-3,4-dihydroquinazolin-7-yl)-3-(4-methylpiperazin-1-yl)propanamide, N-[3,4-Dihydro-3-[[4-hydroxy-1-[(3R)-1-oxo-3-phenylbutyl]-4-piperidinyl]methyl]-4-oxo-7-quinazolinyl]-4-methyl-1-piperazinepropanamide, XL-188

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关于此项目

经验公式（希尔记法）:
C32H42N6O4
化学文摘社编号:
2305045-76-3
分子量:
574.71
UNSPSC Code:
12352200
NACRES:
NA.77

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产品名称

XL188, ≥98% (HPLC)

InChI

1S/C32H42N6O4/c1-24(25-6-4-3-5-7-25)20-30(40)37-14-11-32(42,12-15-37)22-38-23-33-28-21-26(8-9-27(28)31(38)41)34-29(39)10-13-36-18-16-35(2)17-19-36/h3-9,21,23-24,42H,10-20,22H2,1-2H3,(H,34,39)/t24-/m1/s1

InChI key

QLBYDWATOPNXBG-XMMPIXPASA-N

SMILES string

O=C1N(CC2(O)CCN(C(C[C@@H](C)C3=CC=CC=C3)=O)CC2)C=NC4=CC(NC(CCN5CCN(C)CC5)=O)=CC=C41

assay

≥98% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 2 mg/mL, clear

storage temp.

2-8°C

Quality Level

100

相关类别

Biochem/physiol Actions

Highly selective and potent (IC50 90 nM) non covalent inhibitor of USP7
XL188 is a highly selective and potent (IC50 90 nM) non covalent inhibitor of USP7 that binds to the USP7 active site. XL188 facilitates degradation of HDM2, and increases the levels of p53 and p21 in MCF7 cells.

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number
0000179540
0000179541
0000167601
0000167601
0000179541

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Ilaria Lamberto et al.
Cell chemical biology, 24(12), 1490-1500 (2017-10-24)
Deubiquitinating enzymes (DUBs) have garnered significant attention as drug targets in the last 5-10 years. The excitement stems in large part from the powerful ability of DUB inhibitors to promote degradation of oncogenic proteins, especially proteins that are challenging to
Björn Stolte et al.
The Journal of experimental medicine, 215(8), 2137-2155 (2018-07-27)
Ewing sarcoma is a pediatric cancer driven by EWS-ETS transcription factor fusion oncoproteins in an otherwise stable genomic background. The majority of tumors express wild-type TP53, and thus, therapies targeting the p53 pathway would benefit most patients. To discover targets
Jonathan W Bushman et al.
Cell chemical biology, 28(1), 78-87 (2020-10-03)
Deubiquitinating enzymes (DUBs) catalyze the removal of ubiquitin, thereby reversing the activity of E3 ubiquitin ligases and are central to the control of protein abundance and function. Despite the growing interest in DUBs as therapeutic targets, cellular functions for DUBs

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