Recombinant Human DNA Polymerase beta protein
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Recombinant Human DNA Polymerase beta protein is a Human Full Length protein, in the 2 to 335 aa range, expressed in Escherichia coli, with >84%, suitable for SDS-PAGE.
View Alternative Names
DNA polymerase beta, 5'-deoxyribose-phosphate lyase, AP lyase, 5'-dRP lyase, POLB
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human DNA Polymerase beta protein (AB196082)
4-20% SDS-PAGE analysis of 2.6 μg ab196082 with Coomassie staining.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
DNA polymerase beta helps to maintain genome integrity by repairing DNA lesions caused by oxidation alkylation or deamination. This protein often collaborates with other components of the DNA repair pathways but it does not directly form a larger protein complex focusing instead on its important function in BER. When DNA damage like single-strand breaks occur pol β carries out important gap-filling synthesis steps preparing the strand for subsequent ligation.
Pathways
DNA polymerase beta functions critically in base excision repair and acts alongside other important proteins like XRCC1. The BER pathway operates to correct DNA damage from endogenous sources preventing harmful mutations. This pathway is essential for maintaining cellular stability and protecting cells from apoptosis or malignant transformation that might occur if DNA damage propagates.
Specifications
Form
Liquid
General info
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).
Sequence similarities
Belongs to the DNA polymerase type-X family.
Post-translational modifications
Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.. Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin, leading to degradation by the proteasome. USP47 mediates the deubiquitination of monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP and its subsequent degradation.
Subcellular localisation
Nucleus
Target data
Complementary Products
Product promise
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