DNA Polymerase β Antibody
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, IHC |
---|---|
Primary Accession | P06746 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | polyclonal |
Calculated MW | 38178 Da |
Gene ID | 5423 |
---|---|
Other Names | DNA polymerase beta, 4299-, POLB |
Dilution | WB~~1:1000 IHC~~1:50-1:100 |
Format | Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.09% (W/V) sodium azide and 50% glycerol. |
Storage Conditions | -20℃ |
Name | POLB |
---|---|
Function | Repair polymerase that plays a key role in base-excision repair (PubMed:10556592, PubMed:9207062, PubMed:9572863). During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap (PubMed:10556592, PubMed:17526740, PubMed:9556598, PubMed:9572863, PubMed:9614142). Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase (PubMed:9614142). |
Cellular Location | Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage |
For Research Use Only. Not For Use In Diagnostic Procedures.

Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
REFERENCES
Patterson T.A.,et al.Protein Expr. Purif. 18:100-110(2000).
Dobashi Y.,et al.Hum. Genet. 95:389-390(1995).
Chyan Y.-J.,et al.Nucleic Acids Res. 22:2719-2725(1994).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Halleck A.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.

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