SML2786
WRG-28
≥98% (HPLC)
Sinônimo(s):
DDR2 inhibitor WRG-28, N-Ethyl-4-[[(3-oxo-3H-phenoxazin-7-yl)oxy]methyl]-benzenesulfonamide
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About This Item
Produtos recomendados
Nível de qualidade
Ensaio
≥98% (HPLC)
forma
powder
cor
white to very dark orange
solubilidade
DMSO: 2 mg/mL, clear
temperatura de armazenamento
2-8°C
Ações bioquímicas/fisiológicas
WRG-28 is a potent, selective and extracellularly acting allosteric inhibitor of discoidin domain receptor 2 (DDR2) that potently inhibits invasion and migration in mice model of breast cancer. WRG-28 inhibits metastatic breast tumor cell colonization in the lungs.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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Tomography (Ann Arbor, Mich.), 5(1), 53-60 (2019-03-12)
Histone deacetylases regulate a wide variety of cellular functions and have been implicated in redifferentiation of various tumors. Histone deacetylase inhibitors (HDACi) are potential pharmacologic agents to improve outcomes for patients with gliomas. We assessed the therapeutic efficacy of belinostat
Artificial cells, nanomedicine, and biotechnology, 47(1), 3955-3960 (2019-10-02)
Belinostat is a histone deacetylase inhibitor drug capable of regulating cell growth in diverse cancers. Nonetheless, little information clarified the role of Belinostat in breast cancer. Hence, the functions of Belinostat in breast cancer cells survival was disclosed in this
Journal of inorganic biochemistry, 206, 110981-110981 (2020-02-24)
Vorinostat (suberoylanilide hydroxamic acid; SAHA) and Belinostat are two hydroxamate-based histone deacetylase inhibitors that are used clinically as potent anti-cancer agents. Their metabolic breakdown into inactive metabolites such as carboxylic acid and glucuronic derivatives results in them having short half-lives
Nature communications, 11(1), 2086-2086 (2020-05-01)
Gain of function (GOF) DNA binding domain (DBD) mutations of TP53 upregulate chromatin regulatory genes that promote genome-wide histone methylation and acetylation. Here, we therapeutically exploit the oncogenic GOF mechanisms of p53 codon 158 (Arg158) mutation, a DBD mutant found
British journal of haematology, 188(2), 295-308 (2019-08-28)
Ixazomib activity and transcriptomic analyses previously established in T cell (TCL) and Hodgkin (HL) lymphoma models predicted synergistic activity for histone deacetylase (HDAC) inhibitory combination. In this present study, we determined the mechanistic basis for ixazomib combination with the HDAC
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