PTMScan® Symmetric Di-Methyl Arginine Motif [sdme-RG] Kit #13563
Additional Information
This product is intended for peptide enrichment and mass spectrometry analysis. To learn more about our Proteomics Kits and Services please answer a few questions for our Proteomics group.
Product Information
Product Usage Information
Cells are lysed in a urea-containing buffer, cellular proteins are digested by proteases, and the resulting peptides are purified by reversed-phase solid-phase extraction. Peptides are then subjected to immunoaffinity purification using a PTMScan® Motif Antibody conjugated to protein A agarose beads. Unbound peptides are removed through washing, and the captured PTM-containing peptides are eluted with dilute acid. Reversed-phase purification is performed on microtips to desalt and separate peptides from antibody prior to concentrating the enriched peptides for LC-MS/MS analysis. CST recommends the use of PTMScan® IAP Buffer #9993 included in the kit.
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Product Description
Background
In undifferentiated mouse embryonic neural precursors, symmetrically dimethylated histone H4R3 is prevalent, but in later stages of development, both symmetric and asymmetric dimethyl H4R3 modifications are detected in post-mitotic neurons and developing oligodendrocytes. This implies that sDMA modifications may be negative epigenetic regulatory events while aDMA modifications may signal epigenetic activation sites (7).
- Bedford, M.T. and Richard, S. (2005) Mol Cell 18, 263-72.
- Pahlich, S. et al. (2006) Biochim Biophys Acta 1764, 1890-903.
- Bedford, M.T. and Clarke, S.G. (2009) Mol Cell 33, 1-13.
- McBride, A.E. and Silver, P.A. (2001) Cell 106, 5-8.
- Gary, J.D. and Clarke, S. (1998) Prog Nucleic Acid Res Mol Biol 61, 65-131.
- Cheng, D. et al. (2007) Mol Cell 25, 71-83.
- Chittka, A. (2010) PLoS One 5, e13807.
Product Citations: 2
Limited Uses
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