Benzoyl Lysine (F5U6Z) Rabbit mAb #36723
- WB
Supporting Data
| REACTIVITY | All |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- All-All Species Expected
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
Kbz was initially discovered on histone proteins, yet Kbz-modified substrates extend into non-histone substrates, including alcohol dehydrogenase B (AdhB) in A. flavus and ATP-citrate lyase (ACLY) in humans (4,5,8). In the former case, AdhB competes with aflatoxin generation by converting the aflatoxin precursor acetaldehyde to ethanol. Mutation of a Kbz-modified site on AdhB to a non-lysine residue prevents Kbz formation and attenuates AdhB enzymatic activity, leading to increased aflatoxin production by the fungus (4). In the latter case, treating cells with sodium benzoate to elevate ACLY benzoylation or expressing an ACLY transgene encoded with a Kbz site using non-natural amino acids leads to reduced ACLY enzymatic activity (5).
- Lennerz, B.S. et al. (2015) Mol Genet Metab 114, 73-9.
- Heider, J. and Fuchs, G. (1997) Eur J Biochem 243, 577-96.
- Tan, D. et al. (2022) iScience 25, 105443.
- Chen, X. et al. (2025) mBio 16, e0266524.
- Peng, P. et al. (2024) iScience 27, 111176.
- Wang, D. et al. (2022) Nat Commun 13, 1369.
- Li, D. et al. (2024) Ecotoxicol Environ Saf 270, 115877.
- Huang, H. et al. (2018) Nat Commun 9, 3374.
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