|Other Names||DNA polymerase lambda, Pol Lambda, 4299-, DNA polymerase beta-2, Pol beta2, DNA polymerase kappa, POLL|
|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 that functions in several pathways of DNA repair (PubMed:11457865, PubMed:19806195, PubMed:20693240). Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA (PubMed:11457865, PubMed:19806195). Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination (PubMed:19806195, PubMed:20693240). Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities (PubMed:10982892, PubMed:10887191, PubMed:12809503, PubMed:14627824, PubMed:15537631, PubMed:19806195). Has also a 5'-deoxyribose-5- phosphate lyase (dRP lyase) activity (PubMed:11457865, PubMed:19806195).|
|Tissue Location||Expressed in a number of tissues. Abundant in testis|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a DNA polymerase. DNA polymerases catalyze DNA-template-directed extension of the 3'-end of a DNA strand. This particular polymerase, which is a member of the X family of DNA polymerases, likely plays a role in non-homologous end joining and other DNA repair processes.
Brown, J.A., et al. J. Mol. Biol. 395(2):282-290(2010)van Loon, B., et al. Proc. Natl. Acad. Sci. U.S.A. 106(43):18201-18206(2009)Garcia-Diaz, M., et al. Nat. Struct. Mol. Biol. 16(9):967-972(2009)
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