| Form | Liquid |
|---|---|
| Host Species | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Purification | Purified by antigen affinity column. |
| Endotoxin Level | Please contact with the lab for this information. |
| Applications | ELISA, IHC, WB |
| Species Reactivity | Mouse, Human |
| Target | DGU, EC:3.2.2.27, UDG, UNG, UNG1, UNG15, Uracil-DNA glycosylase |
| Immunogen | E. coli - derived recombinant Mouse UNG (Ser60-Leu306). |
| Storage Buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. |
| Product Usage Information | ELISA:1:5000-1:20000;IHC:1:50-1:500;WB:1:500-1:2000 |
| Accession Number | P97931 |
| Background | Uracil-DNA glycosylase (UNG) is a ~33 kDa protein. Uracil-DNA glycosylase that hydrolyzes the N-glycosidic bond between uracil and deoxyribose in single- and double-stranded DNA (ssDNA and dsDNA) to release a free uracil residue and form an abasic (apurinic/apyrimidinic; AP) site. Excises uracil residues arising as a result of misincorporation of dUMP residues by DNA polymerase during replication or due to spontaneous or enzymatic deamination of cytosine. Mediates error-free base excision repair (BER) of uracil at replication forks. According to the model, it is recruited by PCNA to S-phase replication forks to remove misincorporated uracil at U:A base mispairs in nascent DNA strands. Via trimeric RPA it is recruited to ssDNA stretches ahead of the polymerase to allow detection and excision of deaminated cytosines prior to replication. 1. Torseth, K. et al. (2012) DNA repair 11, 559-69. PMID: 22521144 2. Nilsen, H. et al. (1997) Nucleic acids research 25, 750-5. PMID: 9016624 3. Rada, C. et al. (2002) Current biology : CB 12, 1748-55. PMID: 12401169 4. Maul, RW. et al. (2011) Nature immunology 12, 70-6. PMID: 21151102 5. Schrader, CE. et al. (2005) The Journal of experimental medicine 202, 561-8. PMID: 16103411 |
| Note | For research use only |