POLL Antibody, Biotin conjugated

1. Bond formation and cleavage reactions catalyzed by base excision repair DNA polymerases beta and lambda has been described. PMID: 27992186
2. When mutated or deregulated, DNA polymerase lambda can also be a source of genetic instability. Its multiple roles in DNA damage tolerance and its ability in promoting tumor progression make it also a possible target for novel anticancer approaches. [review] PMID: 28841305
3. Data suggest that individuals who carry the rs3730477 POLL germline variant have an increased risk of estrogen-associated breast cancer. PMID: 27621267
4. T204 was identified as a main target for ATM/DNA-PKcs phosphorylation on human POLL, and this phosphorylation may facilitate the repair of a subset of IR-induced DSBs and the efficient POLL-mediated gap-filling during NHEJ. POLL phosphorylation might favor POLL interaction with the DNA-PK complex at DSBs. PMID: 28109743
5. The authors demonstrate that Pol lambda has a flexible active site that can tolerate 8-oxo-dG in either the anti- or syn-conformation. Importantly, we show that discrimination against the pro-mutagenic syn-conformation occurs at the extension step and identify the residue responsible for this selectivity. PMID: 27481934
6. Pol beta, to a greater extent than Pol lambda can incorporate rNMPs opposite normal bases or 8-oxo-G, and with a different fidelity. Further, the incorporation of rNMPs opposite 8-oxo-G delays repair by DNA glycosylases. PMID: 26917111
7. Fen1 significantly stimulated trinucleotide repeats expansion by Pol beta, but not by the related enzyme Pol lambda. PMID: 25687118
8. DNA polymerase lamda catalyzes lesion bypass across benzo[a]pyrene-derived DNA adducts. PMID: 25460917
9. pol lambda is responsible for a significant fraction of Fapy.dG-induced G --> T mutations. PMID: 25741586
10. Structural basis for the binding and incorporation of nucleotide analogs with L-stereochemistry by human DNA polymerase lambda. PMID: 25015085
11. A specific N-terminal extension of the 8 kDa domain of DNA polymerase lambda is important for the non-homologous end joining function. PMID: 23935073
12. Inactivation of polymerase (DNA directed) lambda lyase activity by 5'-(2-phosphoryl-1,4-dioxobutane prevents the enzyme from conducting polymerization following preincubation of the protein and DNA. PMID: 23330920
13. The results provides evidence that DNA pol lambda is required for cell cycle progression and is functionally connected to the S phase DNA damage response machinery in cancer cells. PMID: 23118481
14. A structural study shows how a ribonucleotide can be accommodated in the DNA polymerase lambda active site. PMID: 22584622
15. Results reveal that DNA pol lambda and DNA ligase I are sufficient to promote efficient microhomology-mediated end-joining repair of broken DNA ends in vitro. PMID: 22373917
16. Both Pol lambda- and (Pol kappa)-positive staining were associated with shorter survival in glioma patients. PMID: 20164241
17. Pollambda may play a specialized role in the process of repair of these kinds of lesions PMID: 22317757
18. Studies indicate that pol lambda undergoes posttranslational modifications during the cell cycle that regulate its stability and possibly its subcellular localization. PMID: 21486570
19. In vitro gap-directed translesion DNA synthesis of an abasic site involving human DNA polymerases epsilon, lambda, and beta. PMID: 21757740
20. Studies indicate that codon-based models of gene evolution yielded statistical support for the recurrent positive selection of five NHEJ genes during primate evolution: XRCC4, NBS1, Artemis, POLlambda, and CtIP. PMID: 20975951
21. study found expression of PollambdaR438W sensitizes cells to camptothecin by affecting the homologous recombination pathway, whereas overexpression of pollambdaWT did not impact cell survival; this effect depends entirely on its DNA polymerase activity PMID: 20693240
22. both pol lambda and pol beta interact with the upstream DNA glycosylases for repair of alkylated and oxidized DNA bases PMID: 20805875
23. The fidelity of Pol lambda was maintained predominantly by a single residue, R517, which has minor groove interactions with the DNA template. PMID: 20851705
24. The results demonstrate that loop 1 is not essential for catalytic activity, but it is important for the fidelity of DNA synthesis and the accuracy of non-homologous end joining. PMID: 20435673
25. DNA polymerase lambda can bypass a thymine glycol lesion on the template strand of gapped DNA substrates. PMID: 20423048
26. analysis of the interaction between DNA Polymerase lambda and anticancer nucleoside analogs PMID: 20348107
27. a natural mutator variant of human DNA polymerase lambda promotes chromosomal instability by compromising NHEJ PMID: 19806195
28. DNA polymerase lambda uses a novel sugar selection mechanism to discriminate against ribonucleotides, whereby the ribose 2'-hydroxyl group was excluded mostly by a backbone segment and slightly by the side chain of Y505. PMID: 19900463
29. role in DNA repair PMID: 11821417
30. role in dna replication and DNA repair PMID: 11974915
31. complex between PCNA and pol lambda may play an important role in the bypass of abasic sites in human cells PMID: 12368291
32. DNA polymerase lambda has an intrinsic terminal deoxyribonucleotidyl transferase activity that preferentially adds pyrimidines onto 3'OH ends of DNA oligonucleotides and elongates an RNA primer hybridized to a DNA template. PMID: 12683997
33. mammalian Pol lambda has a role in non-homologous end-joining PMID: 12829698
34. Polymerase lambda is the primary gap-filling polymerase for accurate nonhomologous end joining PMID: 14561766
35. pol lambda Phe506Arg/Gly mutants possess very low polymerase and terminal transferase activities as well as greatly reduced abilities for processive DNA synthesis PMID: 14627824
36. fills short-patched DNA gaps in base excision repair pathways and participates in mammalian nonhomologous end-joining pathways to repair double-stranded DNA breaks PMID: 15157109
37. Results link p53 status with POLkappa expression and suggest that loss of p53 function may in part contribute to the observed POLkappa upregulation in human lung cancers. PMID: 15202001
38. A molecular mechanism is suggested for the observed high in vivo rate of frameshift generation by pol lambda and the remarkable ability of pol lambda to promote microhomology pairing between two DNA strands. PMID: 15350147
39. A helix-hairpin-helix domain of DNA polymerase lambda is important for primer binding and/or for proliferating cell nuclear antigen interaction. PMID: 15358682
40. determined that Fyn phosphorylated MAP-2c on tyrosine 67 PMID: 15537631
41. crystal structures of Pol lambda representing three steps in filling a single-nucleotide gap PMID: 15608652
42. Human DNA polymerase kappa, an error-prone enzyme that is up-regulated in lung cancers, induces DNA breaks and stimulates DNA exchanges as well as aneuploidy. PMID: 15665310
43. Results suggest that Pol lambda plays a role in the short-patch base excision repair rather than contributes to the long-patch base excision repair pathway. PMID: 15979954
44. DNA polymerase lambda is phosphorylated in vitro by several cyclin-dependent kinase/cyclin complexes, including Cdk2/cyclin A, in its proline-serine-rich domain. PMID: 16174846
45. DNA polymerase lambda has the ability to create base pair mismatches and human replication protein A can suppress this intrinsic in vitro mutator phenotype. PMID: 16522650
46. DNA polymerase fidelity is controlled not by an accessory protein or a proofreading exonuclease domain but by an internal regulatory domain PMID: 16675458
47. DNA polymerase lambda is unable to differentiate between matched and mismatched termini during the DNA binding step, thus accounting for the relatively high efficiency of mismatch extension. PMID: 16807316
48. Kinetic studies on human DNA polymerase lambda reveal roles of a downstream strand and the 5'-terminal moieties PMID: 17005572
49. The erroneous nucleotide incorporations catalyzed by DNA polymerases lambda and beta as well as the subsequent ligation catalyzed by a DNA ligase during base excision repair are a threat to genomic integrity. PMID: 17321545
50. cloning, expression and tissue distribution in normal liver and hepatoma PMID: 17653665

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HGNC: 9184

OMIM: 606343

KEGG: hsa:27343

STRING: 9606.ENSP00000299206

UniGene: Hs.523230