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SML2911

Sigma-Aldrich

dBRD9 Hydrochloride

≥97% (HPLC)

Synonym(s):

2-[[[4-(1,2-Dihydro-2-methyl-1-oxo-2,7-naphthyridin-4-yl)-2,6-dimethoxyphenyl]methyl]methylamino]-N-[2-[2-[2-[[2-(2,6-dioxo-3-piperidinyl)-2,3-dihydro-1,3-dioxo-1H-isoindol-4-yl]amino]ethoxy]ethoxy]ethyl]acetamide Hydrochloride, Naphthiridinone degrader 6 Hydrochloride

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About This Item

Empirical Formula (Hill Notation):
C40H45N7O10 · xHCl
Molecular Weight:
783.83 (free base basis)
UNSPSC Code:
12352200
NACRES:
NA.77

ligand

pomalidomide

Quality Level

Assay

≥97% (HPLC)

form

powder

storage condition

desiccated

color

white to beige

solubility

H2O: 2 mg/mL, clear

storage temp.

−20°C

Biochem/physiol Actions

dBRD9 is a cell permeable, potent and selective BRD9-directed chemical degrader that bridges the BRD9 bromodomain and the cereblon E3 ubiquitin ligase complex. dBRD9 exhibits a potent anti-proliferative activity in human AML lines.

related product

Product No.
Description
Pricing

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Brittany C Michel et al.
Nature cell biology, 20(12), 1410-1420 (2018-11-07)
Mammalian SWI/SNF chromatin remodelling complexes exist in three distinct, final-form assemblies: canonical BAF (cBAF), PBAF and a newly characterized non-canonical complex (ncBAF). However, their complex-specific targeting on chromatin, functions and roles in disease remain largely undefined. Here, we comprehensively mapped
Gerard L Brien et al.
eLife, 7 (2018-11-16)
Synovial sarcoma tumours contain a characteristic fusion protein, SS18-SSX, which drives disease development. Targeting oncogenic fusion proteins presents an attractive therapeutic opportunity. However, SS18-SSX has proven intractable for therapeutic intervention. Using a domain-focused CRISPR screen we identified the bromodomain of
David Remillard et al.
Angewandte Chemie (International ed. in English), 56(21), 5738-5743 (2017-04-19)
The bromodomain-containing protein BRD9, a subunit of the human BAF (SWI/SNF) nucleosome remodeling complex, has emerged as an attractive therapeutic target in cancer. Despite the development of chemical probes targeting the BRD9 bromodomain, there is a limited understanding of BRD9

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