SML2786
WRG-28
≥98% (HPLC)
Synonym(s):
DDR2 inhibitor WRG-28, N-Ethyl-4-[[(3-oxo-3H-phenoxazin-7-yl)oxy]methyl]-benzenesulfonamide
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About This Item
Empirical Formula (Hill Notation):
C21H18N2O5S
CAS Number:
Molecular Weight:
410.44
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.77
Quality Level
Assay
≥98% (HPLC)
form
powder
color
white to very dark orange
solubility
DMSO: 2 mg/mL, clear
storage temp.
2-8°C
Biochem/physiol Actions
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.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Pengwei Lu et al.
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
Saumya S Gurbani et al.
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
Li Ren Kong et al.
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
Xiaoyan Qiu et al.
Cellular reprogramming, 22(1), 14-21 (2020-02-06)
To improve the isolation efficiency of parthenogenetic embryonic stem cells (pESCs) in mice, it is necessary to optimize the method to increase in vitro developmental competence of mice parthenogenetic blastocysts. Therefore, this study aims to investigate an optimal method for
Frank C Passero et al.
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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