R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
NSUN2 (E6N6I) Rabbit mAb #36103
Filter:
- WB
- IP
- IF
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 100 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Immunofluorescence (Frozen) | 1:100 - 1:400 |
| Immunofluorescence (Immunocytochemistry) | 1:100 - 1:400 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
NSUN2 (E6N6I) Rabbit mAb recognizes endogenous levels of total NSUN2 protein. This antibody is expected to be nuclear based on function; however, potentially non-specific mitochondrial staining has been observed by non-overlapping antigens in liver by immunofluorescence. This antibody may detect a band of unknown identity at 55 kDa in rat cell lines.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human NSUN2 protein.
Background
Chemical modifications of RNA regulate many cellular processes. One particular RNA modification, 5-methylcytosine (5-mC), regulates ribosome assembly, translation, and RNA stability (1). In eukaryotes, this modification is added to RNA by the DNA methyltransferase homologue 2 protein (DNMT2; also known as TRDMT1), and also by members of the NOL1/NOP2/SUN domain (NSUN) family of proteins. NSUN proteins are putative S-adenosylmethionine (SAM)-dependent methyltransferases that carry out their enzymatic activity by utilizing two cysteine residues in their active sites (2). There are currently seven known members of this family, consisting of NOP2 (NSUN1) and NSUN2-7.
NSUN2 is an 86 kDa member of the NSUN family that is predominantly localized to the nucleus and methylates a variety of tRNAs and other RNA substrates (3). NSUN2 has been found to play a role in the methylation of pre-tRNALeu, tRNAGly, tRNAVal, tRNALeu, and tRNAAsp (1,4,5). It has also been found to methylate mRNAs and several ncRNAs, such as vtRNAs (6-8). Elevated NSUN2 protein levels have been reported in multiple types of human cancers, including breast, prostate, kidney, bladder, and liver, among others (9). The methyltransferase activity of NSUN2 is reduced upon Aurora B kinase-mediated phosphorylation at Ser139 (10), and there is potential for NSUN2 to be used as a therapeutic target or diagnostic marker for Aurora B linked cancers (9).
NSUN2 is an 86 kDa member of the NSUN family that is predominantly localized to the nucleus and methylates a variety of tRNAs and other RNA substrates (3). NSUN2 has been found to play a role in the methylation of pre-tRNALeu, tRNAGly, tRNAVal, tRNALeu, and tRNAAsp (1,4,5). It has also been found to methylate mRNAs and several ncRNAs, such as vtRNAs (6-8). Elevated NSUN2 protein levels have been reported in multiple types of human cancers, including breast, prostate, kidney, bladder, and liver, among others (9). The methyltransferase activity of NSUN2 is reduced upon Aurora B kinase-mediated phosphorylation at Ser139 (10), and there is potential for NSUN2 to be used as a therapeutic target or diagnostic marker for Aurora B linked cancers (9).
- Trixl, L. and Lusser, A. (2019) Wiley Interdiscip Rev RNA 10, e1510.
- Bohnsack, K.E. et al. (2019) Genes (Basel) 10, pii: E102. doi: 10.3390/genes10020102.
- Bourgeois, G. et al. (2015) PLoS One 10, e0133321.
- Brzezicha, B. et al. (2006) Nucleic Acids Res 34, 6034-43.
- Tuorto, F. et al. (2012) Nat Struct Mol Biol 19, 900-5.
- Tang, H. et al. (2015) Aging (Albany NY) 7, 1143-58.
- Xing, J. et al. (2015) Mol Cell Biol 35, 4043-52.
- Hussain, S. et al. (2013) Cell Rep 4, 255-61.
- Okamoto, M. et al. (2012) DNA Cell Biol 31, 660-71.
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