SML1817
BCI-121
≥98% (HPLC)
Sinônimo(s):
4-(Aminocarbonyl)-N-(4-bromophenyl)-1-piperidineacetamide, BCI121
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About This Item
Fórmula empírica (Notação de Hill):
C14H18BrN3O2
Número CAS:
Peso molecular:
340.22
Código UNSPSC:
12352200
NACRES:
NA.77
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Nível de qualidade
Ensaio
≥98% (HPLC)
forma
powder
cor
white to beige
solubilidade
DMSO: 20 mg/mL, clear
temperatura de armazenamento
2-8°C
Ações bioquímicas/fisiológicas
BCI-121 is a substrate-competitive SMYD3 inhibitor that reduces nuclear histone H3 lys4 di- and tri-methylation level (by 50%/H3K4me2 and 40%H3K4me3 in HT29 cells; 100 μM BCI-121 for 48 h), downregulates known SMYD3 target genes transcription, and selectively affects SMYD3-dependent proliferation of cancer cultures (46%/HT29 and 54%/HCT116 proliferation reduction; 100 μM BCI-121 for 72 h) with little antiproliferation efficacy toward low SMYD3-expressing cancer cells. BCI-121 targets SMYD3 via direct affinity interaction (kon 357.7/M/s; koff 4.23×10-3/s; KD=koff/kon = 11.8 μM) and effectively competes against histone for SMYD3 binding (%inhibition/[histone H4 peptide]:[BCI-121] ratio = 36.5%/1:1 and 51.0%/1:2.5).
BCI121 is capable of reducing the mesenchymal signature of MDA-MB-231 cells. It can also decrease their ability to invade in vitro and in vivo.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
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SMYD3 promotes the epithelial-mesenchymal transition in breast cancer
Fenizia C, et al.
Nucleic Acids Research, 47(3), 1278-1293 (2018)
Tianjiao Lyu et al.
International journal of cancer, 146(6), 1553-1567 (2019-09-11)
Detachment of cancer cells from the primary tumor and formation of spheroids in ascites is required for implantation metastasis in epithelial ovarian cancer (EOC), but the underlying mechanism of this process has not been thoroughly elucidated. To mimic this process
Ryuji Hamamoto et al.
Cancer science, 107(4), 377-384 (2016-01-12)
Protein methylation is one of the important post-translational modifications. Although its biological and physiological functions were unknown for a long time, we and others have characterized a number of protein methyltransferases, which have unveiled the critical functions of protein methylation
Alessia Peserico et al.
Journal of cellular physiology, 230(10), 2447-2460 (2015-03-03)
SMYD3 is a histone lysine methyltransferase that plays an important role in transcriptional activation as a member of an RNA polymerase complex, and its oncogenic role has been described in different cancer types. We studied the expression and activity of
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