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SML3043

Sigma-Aldrich

XL188

≥98% (HPLC)

Synonym(s):

((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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About This Item

Empirical Formula (Hill Notation):
C32H42N6O4
CAS Number:
Molecular Weight:
574.71
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

Assay

≥98% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 2 mg/mL, clear

storage temp.

2-8°C

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

Biochem/physiol Actions

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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