ALKBH1 antibody
Source Reactivity Background References- Product Name
- ALKBH1 antibody
- Chemical Name
- ALKBH1 antibody
- Synonyms
- ALKBH1 antibody
- CBNumber
- CB85595846
- Formula Weight
- 0
- MOL File
- Mol file
ALKBH1 antibody Chemical Properties,Usage,Production
Source
Rabbit
Reactivity
Human;Monkey
Background
AlkB is an oxidative dealkylating DNA repair enzyme first characterized in E.coli. Nine AlkB homologs exist in mammals, with the first eight designated as ALKBH1-ALKBH8, and the ninth as FTO. ALKBH1, which features the highest sequence identity to E.coli AlkB, is an Fe(II) and 2-oxoglutarate-dependent dioxygenase that acts upon nucleic acids such as DNA and tRNA and carries out a wide range of enzymatic functions. Similar to other AlkB proteins, ALKBH1 is able to repair alkylated single-stranded DNA and RNA containing 3-methylcytosine, albeit with weak activity. Perhaps more importantly, it has also been shown to catalyze the demethylation of N1-methyladenosine on tRNAs to regulate translation. ALKBH1 functions in the mitochondria as well, recognizing and oxidizing 5-methylcytosine on mitochondrial tRNAMet to generate 5-formylcytosine, consequently enhancing mitochondrial translation. Interestingly, ALKBH1 has also been shown to possess apurinic/apyrimidinic lyase activity, cleaving both single-stranded and double-stranded DNA at abasic sites, with greatest affinity toward double-stranded DNA with two abasic sites. Lastly, ALKBH1 has been reported to possess N(6)-methyladenine demethylase activity, suggesting a role in epigenetic regulation. However, an additional study was unable to show definitive ALKBH1 6mA demethylase activity using both biochemistry assays and knockout mice, so this enzymatic function remains controversial.
References
[1] Samson, L. and Cairns, J. (1977) Nature 267, 281-3.
[2] Chen, B.J. et al. (1994) J Bacteriol 176, 6255-61.
[3] Aravind, L. and Koonin, E.V. (2001) Genome Biol 2, RESEARCH0007.
[4] Trewick, S.C. et al. (2002) Nature 419, 174-8.
[5] Falnes, P.Ø. et al. (2002) Nature 419, 178-82.
[6] Fedeles, B.I. et al. (2015) J Biol Chem 290, 20734-42.
[7] Müller, T.A. et al. (2018) Biochem Biophys Res Commun 495, 98-103.
[8] Westbye, M.P. et al. (2008) J Biol Chem 283, 25046-56.
[9] Liu, F. et al. (2016) Cell 167, 816-828.e16.
[10] Haag, S. et al. (2016) EMBO J 35, 2104-19.
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