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Human Polyclonal POLL Primary Antibody for EIA, WB - ABIN951932
Brown, Fiala, Fowler, Sherrer, Newmister, Duym, Suo: A novel mechanism of sugar selection utilized by a human X-family DNA polymerase. in Journal of molecular biology 2010
Show all 3 references for ABIN951932
Human Polyclonal POLL Primary Antibody for IHC (p), IHC - ABIN250110
García-Díaz, Bebenek, Sabariegos, Domínguez, Rodríguez, Kirchhoff, García-Palomero, Picher, Juárez, Ruiz, Kunkel, Blanco: DNA polymerase lambda, a novel DNA repair enzyme in human cells. in The Journal of biological chemistry 2002
Cow (Bovine) Polyclonal POLL Primary Antibody for WB - ABIN2785955
Picher, Blanco: Human DNA polymerase lambda is a proficient extender of primer ends paired to 7,8-dihydro-8-oxoguanine. in DNA repair 2007
DNA Pol lambda recognizes 8-Oxo-G on a template as a normal guanine and preferentially incorporates dCTP over dATP opposite this lesion.
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 Antibodies)-conformation. Importantly, we show that discrimination against the pro-mutagenic syn (show FYN Antibodies)-conformation occurs at the extension step and identify the residue responsible for this selectivity.
Pol beta (show POLB Antibodies), 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 Antibodies) significantly stimulated trinucleotide repeats expansion by Pol beta (show POLB Antibodies), but not by the related enzyme Pol lambda.
DNA polymerase (show POLB Antibodies) 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.
A structural study shows how a ribonucleotide can be accommodated in the DNA polymerase lambda active site.
Pol mu (show POLM Antibodies) 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 Antibodies)) with no effect on mutation specificity, suggesting no direct role in SHM (show CNTNAP1 Antibodies).
both pol lambda and pol beta (show POLB Antibodies) 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 (show POLM Antibodies) 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