Product Pathways - Screening Technologies
Symmetric Di-Methyl Arginine Motif [sdme-RG] MultiMab™ Rabbit mAb mix #13222
|13222S||100 µl ( 10 western blots )||￥3,250.00||现货查询 购买询价 防伪查询|
|13222||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting,
Specificity / Sensitivity
Symmetric Di-Methyl Arginine Motif [sdme-RG] Rabbit mAb recognizes endogenous levels of proteins that are symmetrically dimethylated on arginine residues. This antibody does not cross-react with monomethylated, asymmetrically methylated arginine, or methylated lysine residues.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide library containing the symmetric dimethyl-arginine [sdme-RG] motif. The antibody is a mix of two monoclonal antibodies to elicit broad reactivity while maintaining specificity.
Western blot analysis of MCF7 cells, untreated (-) or treated with Adenosine-2', 3'-dialdehyde (AdOx, 100 μM, 24 hr; +) using Symmetric Di-Methyl Arginine Motif [sdme-RG] Rabbit mAb (upper) or GAPDH (D16H11) XP® Rabbit mAb #5174 (lower).
The specificity of Symmetric Di-Methyl Arginine Motif [sdme-R] Rabbit mAb was determined by peptide ELISA. The figure demonstrates that the antibody is specific for Symmetric Di-Methyl Arginine and does not react with mono-methyl, di-methyl or tri-methyl lysine and does not react with mono-methyl or asymmetric di-methyl arginine.
Arginine methylation is a prevalent PTM found on both nuclear and cytoplasmic proteins. Arginine methylated proteins are involved in many different cellular processes, including transcriptional regulation, signal transduction, RNA metabolism, and DNA damage repair (1-3). Arginine methylation is carried out by the arginine N-methyltransferase (PRMT) family of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (4). There are three different types of arginine methylation: asymmetric dimethylarginine (aDMA, omega-NG,NG-dimethylarginine), where two methyl groups are placed on one of the terminal nitrogen atoms of the guanidine group of arginine; symmetric dimethylarginine (sDMA, omega-NG,N’G-dimethylarginine), where one methyl group is placed on each of the two terminal guanidine nitrogens of arginine; and monomethylarginine (MMA, omega-NG-dimethylarginine), where a single methyl group is placed on one of the terminal nitrogen atoms of arginine. Each of these modifications has potentially different functional consequences. Though all PRMT proteins catalyze the formation of MMA, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce aDMA, while Type II PRMTs (PRMT5 and 7) produce sDMA. Methylated arginine residues often reside in glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (5). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within proline-glycine-methionine rich (PGM) motifs (6).
Symmetrically dimethylated (sDMA) histone H4R3 is prevalent in undifferentiated mouse embryonic neural precursors, but both symmetric and asymmetric dimethyl (aDMA) H4R3 modifications are detected in post-mitotic neurons and developing oligodendrocytes during later stages of development. 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.
- Dhar, S. et al. (2013) Sci Rep 3, 1311.Applications:Western Blotting,
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For Research Use Only. Not For Use In Diagnostic Procedures.
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U.S. Pat. No. 9,085,609
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
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