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Biological Activity for RG 108
RG 108 is a non-nucleoside DNA methyltransferase inhibitor that blocks the enzyme active site. Inhibits DNA methylation in human cancer cell lines in vitro without detectable toxicity. Demethylates and reactivates epigenetically silenced tumor suppressor genes. Enhances the efficiency of induced pluripotent stem cell (iPS) generation.
Compound Libraries for RG 108
Technical Data for RG 108
|Storage||Store at RT|
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
Solubility Data for RG 108
|Solvent||Max Conc. mg/mL||Max Conc. mM|
Preparing Stock Solutions for RG 108
The following data is based on the product molecular weight 334.33. Batch specific molecular weights may vary from batch to batch due to the degree of hydration, which will affect the solvent volumes required to prepare stock solutions.
|Concentration / Solvent Volume / Mass||1 mg||5 mg||10 mg|
|1 mM||2.99 mL||14.96 mL||29.91 mL|
|5 mM||0.6 mL||2.99 mL||5.98 mL|
|10 mM||0.3 mL||1.5 mL||2.99 mL|
|50 mM||0.06 mL||0.3 mL||0.6 mL|
References for RG 108
References are publications that support the biological activity of the product.
Brueckner et al (2005) Epigenetic reactivation of tumor suppressor genes by a novel small-molecule inhibitor of DNA methyltransferase. Cancer Res. 65 6305 PMID: 16024632
Stresemann et al (2006) Functional diversity of DNA methyltransferase inhibitors in human cancer cell lines. Cancer Res. 66 2794 PMID: 16510601
Schirrmacher et al (2006) Synthesis and in vitro evaluation of biotinylated RG108: a high affinity compound for studying binding interactions with human DNA methyltransferases. Bioconjug.Chem. 17 261 PMID: 16536454
If you know of a relevant reference for RG 108, please let us know.
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Keywords: RG 108, RG 108 supplier, Non-nucleoside, DNA, methyltransferase, inhibitor, inhibitors, transferases, RG108, inhibits, methylation, dnmt, epigenetics, Methyltransferases, Stem, Cell, Reprogramming, 3295, Tocris Bioscience
3 Citations for RG 108
Citations are publications that use Tocris products. Selected citations for RG 108 include:
Zhang et al (2016) Pharmacological reprogramming of fibroblasts into neural stem cells by signaling-directed transcriptional activation. Cell Stem Cell 18 653 PMID: 27133794
Nugent et al (2015) Brain feminization requires active repression of masculinization via DNA methylation. PLoS One 18 690 PMID: 25821913
Kottakis et al (2016) LKB1 loss links serine metabolism to DNA methylation and tumorigenesis. Nature 539 390 PMID: 27799657
Do you know of a great paper that uses RG 108 from Tocris? Please let us know.
Reviews for RG 108
Average Rating: 5 (Based on 2 Reviews.)
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Cells are treated with 10 µM RG 108
Literature in this Area
Tocris offers the following scientific literature in this area to showcase our products. We invite you to request* your copy today!
*Please note that Tocris will only send literature to established scientific business / institute addresses.
Cell Cycle and DNA Damage Research Product Guide
This product guide provides a review of the cell cycle and DNA damage research area and lists over 170 products, including research tools for:
- Cell Cycle and Mitosis
- DNA Damage Repair
- Targeted Protein Degradation
- Ubiquitin Proteasome Pathway
- Chemotherapy Targets
Epigenetics Scientific Review
Written by Susanne Müller-Knapp and Peter J. Brown, this review gives an overview of the development of chemical probes for epigenetic targets, as well as the impact of these tool compounds being made available to the scientific community. In addition, their biological effects are also discussed. Epigenetic compounds available from Tocris are listed.
Epigenetics Research Bulletin
Produced by Tocris and updated in 2014, the epigenetics research bulletin gives an introduction into mechanisms of epigenetic regulation, and highlights key Tocris products for epigenetics targets including:
- DNA Methyltransferases
- Histone Deacetylases
- Histone Demethylases
- Histone Methyltransferases