TRMT112 Antibody #57540
- WB
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 15 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
TRMT112 Antibody recognizes endogenous levels of total TRMT112 protein. This antibody detects a 20 kDa protein of unknown origin.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro108 of human TRMT112 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Multifunctional methyltransferase subunit TRM112-like protein (TRMT112) is an evolutionarily conserved 15 kDa protein that interacts with and stabilizes various methyltransferases involved in tRNA, rRNA, and protein methylation. While most studies have been in yeast, TRMT112 has been shown to interact with human methyltransferases involved in translation and ribosome biogenesis, including TRMT11, ALKBH8, HEMK2a, WBSCR22, and METTL5 (1-5). TRMT112 is also widely expressed during embryogenesis (6).
The TRMT11-TRMT112 complex deposits 2-methylguanosine at position 10 of tRNA, while ALKBH8-TRMT112 modifies a uridine at position 34 of the anti-codon loop (5,7) Additionally, TRMT112 plays a role in translation termination by interacting with N6AMT1, causing methylation of the release factor eRF1 to allow for stop codon recognition (8,9).
TRMT112 also contributes to ribosome biogenesis by interacting with and stabilizing WBSCR22, an 18s rRNA methyltransferase, and METTL5, the 18s rRNA m6a-methyltransferase (3,4,10).
- Songe-Møller, L. et al. (2010) Mol Cell Biol 30, 1814-27.
- Figaro, S. et al. (2008) FEBS Lett 582, 2352-6.
- van Tran, N. et al. (2019) Nucleic Acids Res 47, 7719-7733.
- Õunap, K. et al. (2015) PLoS One 10, e0133841.
- Purushothaman, S.K. et al. (2005) Mol Cell Biol 25, 4359-70.
- Gu, T. et al. (2012) Acta Histochem Cytochem 45, 113-9.
- Mazauric, M.H. et al. (2010) J Biol Chem 285, 18505-15.
- Pachman, L.M. et al. (2006) Arthritis Rheum 54, 3345-50.
- Heurgué-Hamard, V. et al. (2005) J Biol Chem 280, 2439-45.
- Zorbas, C. et al. (2015) Mol Biol Cell 26, 2080-95.
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