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POLB / DNA Polymerase Beta Antibody (aa286-335)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | P06746 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 38kDa |
| Dilution | ELISA (1:10000), IHC-P (5 µg/ml), WB (1:500-1:1000) |
| Gene ID | 5423 |
|---|---|
| Other Names | DNA polymerase beta, 2.7.7.7, 4.2.99.-, POLB |
| Target/Specificity | DNA Polymerase beta Antibody detects endogenous levels of total DNA Polymerase beta protein. |
| Reconstitution & Storage | Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. |
| Precautions | POLB / DNA Polymerase Beta Antibody (aa286-335) is for research use only and not for use in diagnostic or therapeutic procedures. |
| 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 |
| Volume | 50 µl |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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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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