Recombinant Human DNA polymerase lambda (POLL)

Code CSB-YP871513HU
MSDS
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Source Yeast
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Code CSB-EP871513HU
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Source E.coli
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Code CSB-EP871513HU-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP871513HU
MSDS
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Source Baculovirus
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Code CSB-MP871513HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
POLL
Uniprot No.
Alternative Names
BETA N; BETAN; DNA directed DNA polymerase lambda; DNA polymerase beta 2; DNA polymerase beta-2; DNA polymerase kappa; DNA polymerase kappa DNA polymerase beta N; DNA polymerase lambda; DNA polymerase lamda2; DPOLL_HUMAN; EC 2.7.7.7,EC 4.2.99.; FLJ46002; OTTHUMP00000020321; OTTHUMP00000020323; OTTHUMP00000059179; Pol beta2; POL KAPPA; Pol Lambda; POLKAPPA; POLL; Polymerase DNA directed lambda
Species
Homo sapiens (Human)
Expression Region
1-575
Target Protein Sequence
MDPRGILKAF PKRQKIHADA SSKVLAKIPR REEGEEAEEW LSSLRAHVVR TGIGRARAEL FEKQIVQHGG QLCPAQGPGV THIVVDEGMD YERALRLLRL PQLPPGAQLV KSAWLSLCLQ ERRLVDVAGF SIFIPSRYLD HPQPSKAEQD ASIPPGTHEA LLQTALSPPP PPTRPVSPPQ KAKEAPNTQA QPISDDEASD GEETQVSAAD LEALISGHYP TSLEGDCEPS PAPAVLDKWV CAQPSSQKAT NHNLHITEKL EVLAKAYSVQ GDKWRALGYA KAINALKSFH KPVTSYQEAC SIPGIGKRMA EKIIEILESG HLRKLDHISE SVPVLELFSN IWGAGTKTAQ MWYQQGFRSL EDIRSQASLT TQQAIGLKHY SDFLERMPRE EATEIEQTVQ KAAQAFNSGL LCVACGSYRR GKATCGDVDV LITHPDGRSH RGIFSRLLDS LRQEGFLTDD LVSQEENGQQ QKYLGVCRLP GPGRRHRRLD IIVVPYSEFA CALLYFTGSA HFNRSMRALA KTKGMSLSEH ALSTAVVRNT HGCKVGPGRV LPTPTEKDVF RLLGLPYREP AERDW
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Gene References into Functions
  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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Subcellular Location
Nucleus. Chromosome.
Protein Families
DNA polymerase type-X family
Tissue Specificity
Expressed in a number of tissues. Abundant in testis.
Database Links

HGNC: 9184

OMIM: 606343

KEGG: hsa:27343

STRING: 9606.ENSP00000299206

UniGene: Hs.523230

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