|Description||Rabbit IgG polyclonal antibody for DNA polymerase beta(POLB) detection. Tested with WB in Human.|
|Reconstitution||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Other Names||DNA polymerase beta, 22.214.171.124, 4.2.99.-, POLB|
|Calculated MW||38178 MW KDa|
|Application Details||Western blot, 0.1-0.5 µg/ml, Human|
|Subcellular Localization||Nucleus. Cytoplasm. Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage.|
|Protein Name||DNA polymerase beta|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.|
|Immunogen||E.coli-derived human POLB recombinant protein (Position: L122-E335). Human POLB shares 95.3% and 94.9% amino acid (aa) sequence identity with mouse and rat POLB, respectively.|
|Purification||Immunogen affinity purified.|
|Cross Reactivity||No cross reactivity with other proteins.|
|Storage||At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.|
|Function||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.|
|Cellular Location||Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage|
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Provided below are standard protocols that you may find useful for product applications.
Polymerase (DNA directed), beta, also known as POLB, is an enzyme that, in humans, is encoded by the POLB gene. It is localized on 8p11.2. The protein encoded by this gene is a DNA polymerase involved in base excision and repair, also called gap-filling DNA synthesis. It is found that a truncated POLB is expressed in primary colorectal tumors and inhibits the normal repair function of wildtype POLB. The encoded protein, acting as a monomer, is normally found in the cytoplasm, but it translocates to the nucleus upon DNA damage. Several transcript variants of this gene exist, but the full-length nature of only one has been described to date. Additionally, human POLB forms a complex with and is methylated by PRMT6. In vitro, methylated POLB possesses significantly higher DNA polymerase activity when compared to that of unmodified enzyme. The increase in DNA polymerase activity upon methylation is due to the enhanced DNA binding and processivity of POLB.
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