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DNA Pol lambda recognizes 8-Oxo-G on a template as a normal guanine and preferentially incorporates dCTP over dATP opposite this lesion.
T204 was identified as a main target for ATM (show ATM ELISA Kits)/DNA-PKcs (show PRKDC ELISA Kits) 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.
The authors demonstrate that Pol lambda has a flexible active site that can tolerate 8-oxo-dG in either the anti- or syn (show FYN ELISA Kits)-conformation. Importantly, we show that discrimination against the pro-mutagenic syn (show FYN ELISA Kits)-conformation occurs at the extension step and identify the residue responsible for this selectivity.
Pol beta (show POLB ELISA Kits), 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.
Fen1 (show FEN1 ELISA Kits) significantly stimulated trinucleotide repeats expansion by Pol beta (show POLB ELISA Kits), but not by the related enzyme Pol lambda.
DNA polymerase (show POLB ELISA Kits) lamda catalyzes lesion bypass across benzo[a]pyrene-derived DNA adducts.
pol lambda is responsible for a significant fraction of Fapy.dG-induced G --> T mutations.
Structural basis for the binding and incorporation of nucleotide analogs with L-stereochemistry by human DNA polymerase lambda.
A specific N-terminal extension of the 8 kDa domain of DNA polymerase lambda is important for the non-homologous end joining function.
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.
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.
Pol mu and Pol lambda play a key role in conferring on NHEJ the flexibility required for accurate and efficient repair
Results show that deficiency of either DNA polymerases beta or lambda or both results in a modest but significant decrease in V region somatic hypermutation (SHM (show CNTNAP1 ELISA Kits)) with no effect on mutation specificity, suggesting no direct role in SHM (show CNTNAP1 ELISA Kits).
both pol lambda and pol beta (show POLB ELISA Kits) interact with the upstream DNA glycosylases for repair of alkylated and oxidized DNA bases
analysis of the interaction between DNA Polymerase lambda and anticancer nucleoside analogs
Hydrocephalus, situs inversus, chronic sinusitis, and male infertility in DNA polymerase lambda-deficient mice: possible implication for the pathogenesis of immotile cilia syndrome.
Pol lambda is not required for normal Ig gene hypermutation.
Pol lambda contributes to base excision repair in mouse fibroblast cell extract.
Pol lambda protects cells against oxidative stress, and participates in oxidative DNA damage base excision repair.
third hypervariable region assumes for each immunoglobulin chain, with pol lambda maintaining a large heavy chain junctional heterogeneity and pol mu ensuring a restricted light chain junctional variability
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. Alternatively spliced transcript variants have been described.
DNA polymerase lambda
, DNA-directed DNA polymerase lambda
, polymerase (DNA directed), lambda
, DNA polymerase lambda-like
, DNA polymerase beta-2
, DNA polymerase beta-N
, DNA polymerase kappa
, pol Lambda