|Other Names||DNA polymerase kappa, DINB protein, DINP, POLK, DINB1|
|Target/Specificity||The synthetic peptide sequence is selected from aa 546-560 of HUMAN POLK|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.|
|Cellular Location||Nucleus. Note=Detected throughout the nucleus and at replication foci|
|Tissue Location||Detected at low levels in testis, spleen, prostate and ovary. Detected at very low levels in kidney, colon, brain, heart, liver, lung, placenta, pancreas and peripheral blood leukocytes.|
email@example.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
External and internal DNA-damaging agents continually threaten the integrity of genetic material in cells. Although a variety of repair mechanisms exist to remove the resulting lesions, some lesions escape repair and block the replication machinery. Members of the Y family of DNA polymerases, such as POLK, permit the continuity of the replication fork by allowing replication through such DNA lesions. Each Y family polymerase has a unique DNA-damage bypass and fidelity profile. POLK is specialized for the extension step of lesion bypass (summary by Lone et al., 2007 [PubMed 17317631]).
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Monsees, G.M., et al. Breast Cancer Res. Treat. (2010) In press :
Katafuchi, A., et al. Nucleic Acids Res. 38(3):859-867(2010)
Fukuda, H., et al. J. Biol. Chem. 284(38):25585-25592(2009)
Irimia, A., et al. J. Biol. Chem. 284(33):22467-22480(2009)
If you have any additional inquiries please email technical services at firstname.lastname@example.org.