Product Pathways - Chromatin Regulation / Epigenetics
PRMT6 (D5A2N) Rabbit mAb #14641
|14641S||100 µl ( 10 western blots )||￥3,250.00 现货查询||购买询价|
|14641||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation,
Species predicted to react based on 100% sequence homology: Bovine, S. cerevisiae,
Specificity / Sensitivity
PRMT6 (D5A2N) Rabbit mAb recognizes endogenous levels of total PRMT6 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala62 of human PRMT6 protein.
Western blot analysis of extracts from various cell lines using PRMT6 (D5A2N) Rabbit mAb.
Protein arginine N-methyltransferase 6 (PRMT6) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). The three types of PRMTs share the ability to mono-methylate arginine residues, but vary in their ability to generate differential methylation states (1-3). Mono-methylated arginine residues are further methylated by type I PRMTs to generate an asymmetric di-methyl arginine or by type II PRMTs to form a symmetric-dimethyl arginine. Type III methyltransferases are only able to mono-methylate arginine residues (1-3). PRMT6 is a type I PRMT that acts as both a transcriptional coactivator and a corepressor and catalyzes the asymmetric di-methylation of histone H3 (Arg 2, Arg42), histone H4 (Arg3), and histone H2A at Arg29 (2,4). PRMT6 acts as a coactivator for transcription factors, including estrogen receptor and NFκB, while asymmetric di-methylation of histone H3 (Arg2) by PRMT6 prevents MLL methylation of histone H3 at Lys4 and inhibits transcription activation (5-8). In addition to its role in regulating transcription, PRMT6 methylates DNA polymerase β, leading to enhanced DNA binding and processivity during base excision repair of damaged DNA (9).
- Di Lorenzo, A. and Bedford, M.T. (2011) FEBS Lett 585, 2024-31.
- Yang, Y. and Bedford, M.T. (2013) Nat Rev Cancer 13, 37-50.
- Molina-Serrano, D. et al. (2013) Biochem Soc Trans 41, 751-9.
- Casadio, F. et al. (2013) Proc Natl Acad Sci U S A 110, 14894-9.
- Harrison, M.J. et al. (2010) Nucleic Acids Res 38, 2201-16.
- Di Lorenzo, A. et al. (2014) Nucleic Acids Res 42, 8297-309.
- Hyllus, D. et al. (2007) Genes Dev 21, 3369-80.
- Smith, A.P. et al. (2009) Oncogene 28, 422-30.
- El-Andaloussi, N. et al. (2006) Mol Cell 22, 51-62.
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