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71085 KOD DNA Polymerase

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71085
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
71085-3CN Glass bottle 250 u
Description
OverviewPCR involves replication of a DNA template by a thermostable DNA polymerase. The processivity, specificity, and fidelity of the polymerase enzyme used can influence the efficiency, reproducibility, and yield of the PCR reaction. High-fidelity PCR, utilizes a DNA polymerase with a low error rate and results in a high degree of accuracy in the replication of the DNA of interest. Fidelity is critical when accurate sequence amplification of the gene target is needed, for example, when direct sequencing or cloning for downstream protein expression. Unwarranted mutation could severely impact your studies. Our analysis has shown that KOD enzymes are an easy choice for fast, accurate and high-yielding PCR. EMD Millipore's molecular biologists work to develop and formulate polymerases offering the highest specificity, fidelity and yield during PCR amplification. In addition, optimized buffer compositions, convenient master mixes and cycling parameters provide additional ease of use and data reproducibility. KOD DNA Polymerase (formerly KOD HiFi DNA Polymerase) is a recombinant form of Thermococcus kodakaraensis KOD1 DNA polymerase (Nishioka 2001). KOD is a high fidelity thermostable DNA polymerase that amplifies target DNA up to 6 kbp with superior accuracy and yield for PCR applications (Takagi 1997). The enzyme's 3'→5' exonuclease-dependent proofreading activity results in a lower PCR mutation frequency than any other commercially available DNA polymerase. The elongation rate and processivity are 5 times and 10 to 15 times higher, respectively, than for Pfu DNA polymerase, resulting in highly accurate and robust yield, in a short reaction time. The enzyme generates blunt-ended PCR products suitable for cloning with the Novagen Perfectly Blunt® and LIC Vector Kits.



Source Recombinant Thermococcus kodakaraensis KOD1 DNA polymerase expressed in E. coli
Concentration 2.5 U/µl
Purity > 90% homogeneous by SDS-PAGE
5′ Exonuclease Less than 2% per unit of enzyme when incubated 1 h at 74°C in a reaction with 5′-labeled λ/Sca I digest
Nicking activity None detected
Amplification effiency Functional PCR
Storage –20°C

*Manufactured by Toyobo and distributed by EMD Biosciences, Inc. Not available from EMD Biosciences, Inc. in Japan.

Note: Purchase of this product includes an immunity from suit under patents specified in the product insert to use only the amount purchased for the purchaser's own internal research. No other patents rights (such as 5' Nuclease Process patent rights) are conveyed expressly, by implication, or by estoppel. Further information on purchasing licenses may be obtained by contacting the Director of Licensing, Applied Biosystems, 850 Lincoln Centre Drive, Foster City, California, 94404, USA.

Catalogue Number71085 Brand Family Novagen®
Features and benefits
  • Higher fidelity than Pfu DNA polymerase—excellent for cloning
  • Greater yield—extension speed is 2X faster than Taq DNA polymerase and 5X faster than Pfu DNA polymerase
  • Higher processivity—sequential nucleotide polymerization is 10- to 15-fold greater than Pfu and Tli DNA polymerases
  • Amplifies plasmid and lambda DNA templates up to 6 kbp
  • Amplifies genomic DNA templates up to 2 kbp
  • No truncated amplification products
References
ReferencesNishioka, M., et al. 2001. J. Biotechnol. 88, 141. Takagi, M., et al. 1997. Appl. Environ. Microbiol. 63, 4504.
Product Information
Unit of DefinitionOne unit is defined as the amount of enzyme that will catalyze the incorporation of 10 nmol of dNTP into acid-insoluble form in 30 min at 75°C, in a reaction containing 20 mM Tris-HCl (pH 7.5 at 25°C), 8 mM MgCl₂, 7.5 mM DTT, 50 µg/ml BSA, 150 µM each of dATP, dCTP, dGTP, dTTP (a mix of unlabeled and [<Sup>3</Sup>H]dTTP) and 150 µg/ml activated calf thymus DNA.
250 UKOD DNA Polymerase (2.5 U/µl)
1 ml10X Buffer #1 for KOD DNA Polymerase (pH 8.0)
1 ml10X Buffer #2 for KOD DNA Polymerase (pH 8.8)
1 ml25 mM MgCl₂
1 mldNTP Mix (2 mM each)
DeclarationManufactured by Toyobo and distributed by Novagen. Not available from Novagen in Japan. Purchase of this product is accompanied by a limited license to use it in the Polymerase Chain Reaction (PCR) process for research use in conjunction with a thermal cycler whose use in the automated performance of the PCR process is covered by the up-front license fee, either by payment to Applied Biosystems or as purchased, i.e., an authorized thermal cycler.
Quality LevelMQ100
Applications
Biological Information
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Shipped with Blue Ice or with Dry Ice
Toxicity Standard Handling
Storage -20°C
Do not freeze Ok to freeze
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalogue Number GTIN
71085-3CN 07790788057848

Documentation

KOD DNA Polymerase SDS

Title

Safety Data Sheet (SDS) 

KOD DNA Polymerase Certificates of Analysis

TitleLot Number
71085

References

Reference overview
Nishioka, M., et al. 2001. J. Biotechnol. 88, 141. Takagi, M., et al. 1997. Appl. Environ. Microbiol. 63, 4504.

Brochure

Title
High fidelity gene amplification
PCR Protocols and Guides - Simplify your gene discovery

Citations

Title
  • Palmi T. Atlason, et al. (2007) N-Methyl-D-aspartate (NMDA) receptor subunit NR1 forms the substrate for oligomeric assembly of the NMDA receptor. Journal of Biological Chemistry 282, 25299-25307.
  • Michael A. Calderwood, et al. (2007) Epstein-Barr virus and virus human protein interaction maps. Procedings of the National Academy of Science 104, 7606-7611.
  • Elizabeth E. Crouch, et al. (2007) Regulation of AID expression in the immune response. Journal of Experimental Medicine 204, 1145-1156.
  • Amanda Nga-Sze Mak, et al. (2007) Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site. Nucleic Acids Research 35, 6259-6267.
  • Preeti Malik-Kale, et al. (2007) Characterization of genetically matched isolates of Campylobacter jejuni reveals that mutations in genes involved in flagellar biosynthesis alter the organism's virulence potential. Applied and Enviornmental Microbiology 73, 3123-3136.
  • Dominic Nehme and Keith Poole. (2007) Assembly of the mexAB-oprM multidrug pump of Pseudomonas aeruginosa: component interactions defined by the study of pump mutant suppressors. Journal of Bacteriology 189, 6118-6127.
  • Satoshi Tasumi and Gerardo R. Vasta. (2007) A galectin of unique domain organization from hemocytes of the eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus. Journal of Immunology 179, 3086-3098.
  • J. Wu, et al. (2007) FcαRI (CD89) alleles determine the proinflammatory potential of serum IgA. Journal of Immunology 178, 3973-3982.
  • Hanyi Zhuang and Hiroaki Matsunami. (2007) Synergism of accessory factors in functional expression of mammalian odorant receptors. Journal of Biological Chemistry 282, 15284-15293.
  • Peter J. Atkinson, et al. (2006) Altered expression of Gq/11α protein shapes mGlu1 and mGlu5 receptor-mediated single cell inositol 1,4,5-trisphosphate and Ca2+ signaling. Molecular Pharmacology 69, 174-184.
  • R. Glenn King, Brantley R. Herrin and Louis B. Justement. (2006) Trem-Like Transcript 2 Is Expressed on Cells of the Myeloid/Granuloid and B Lymphoid Lineage and Is Up-Regulated in Response to Inflammation. Journal of Immunology 176, 6012-6021.
  • R. Glenn King, Brantley R. Herrin and Louis B. Justement. (2006) Trem-like transcript 2 is expressed on cells of the myeloid/granuloid and B lymphoid lineage and is up-regulated in response to inflammation. Journal of Immunology 176, 6012-6021.
  • James C. Samuelson, et al. (2006) Engineering a rare-cutting restriction enzyme: genetic screening and selection of NotI variants. Nucleic Acids Research 34, 796-805.
  • Emma L. Walker, Jeffrey L. Bose and Eric V. Stabb. (2006) Photolyase confers resistance to UV light but does not contribute to the symbiotic benefit of bioluminescence in Vibrio fischeri ES114. Applied and Enviornmental Microbiology 72, 6600-6606.
  • Gang Wu, et al. (2006) Simplified gene synthesis: A one-step approach to PCR-based gene construction. Journal of Biotechnology 124, 496-503.
  • Brantley R. Herrin, Alison L. Groeger and Louis B. Justement. (2005) The adaptor protein HSH2 attenuates apoptosis in response to ligation of the B cell antigen receptor complex on the B lymphoma cell line, WEHI-231. Journal of Biological Chemistry 280, (3507-3515).
  • Tom S. Kim, et al. (2005) Delayed dark adaptation in 11-cis-retinol dehydrogenase deficient mice: a role of RDH11 in visual processes in vivo. Journal of Biological Chemistry 280, 8694-8704.
  • Christian Siebold, et al. (2005) High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule. Proceedings of the National Academy of Sciences (USA) 102, 16836-16841.
  • Shinya Kamauchi, et al. (2002) Structurally and Functionally Conserved Domains in the Diverse Hydrophilic Carboxy-Terminal Halves of Various Yeast and Fungal Na+/H+ Antiporters (Nha1p). 131, 821-831.
  • Hitoshi Niwa, et al. (2002) Phenotypic complementation establishes requirements for specific POU domain and generic transactivation function of Oct-3/4 in embryonic stem cells. Molecular and Cellular Biology 22, 1526-1536.
  • Yasushi Ohki, et al. (2002) Role of a conserved J8/7 X P4 base-triple in the Tetrahymena ribozyme. 132, 713-718.
  • Kazuaki Okuno, et al. (2002) An analysis of target preferences of Escherichia coli outer-membrane endoprotease OmpT for use in therapeutic peptide production: efficient cleavage of substrates with basic amino acids at the P4 and P6 positions. Biotechnology and Applied Biochemistry 36, 77-84.
  • Kazuhiro Karaya, Tatsuhito Shimizu and Akira Taketo. (2001) New gene cluster for lantibiotic streptin possibly involved in streptolysin S formation. 129, 769-775.
  • Shigeyuki Kawai, et al. (2001) Molecular characterization of Escherichia coli NAD kinase. European Journal of Biochemistry 268, 4359-4365.
  • Fumitaka Momose, et al. (2001) Cellular splicing factor RAF-2p48/NPI-5/BAT1/UAP56 interacts with the influenza virus nucleoprotein and enhances viral RNA synthesis. Journal of Virology 75, 1899-1908.
  • Kazufumi Yazaki, et al. (2001) A novel Coptis japonica multidrug-resistant protein preferentially expressed in the alkaloid-accumulating rhizome. Journal of Experimental Botany 52, 877-879.
  • Akihiro Matsuura, et al. (2000) NKT cells in the rat: organ-specific distribution of NK T cells expressing distinct Vα14 chains. Journal of Immunology 164, 3140-3148.
  • Kimihiko Hattori, et al. (1999) Molecular dissection of the interactions among IκBα, FWD1, and Skp1 required for ubiquitin-mediated proteolysis of IκBα. Journal of Biological Chemistry 274, 29641-29647.
  • Masatoshi Kitagawa, et al. (1999) An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of β-catenin. European Journal of Biochemistry 18, 2401-2410.
  • Nobutaka Nakashimaa, Eishi Noguchia and Takeharu Nishimotoa. (1999) Saccharomyces cerevisiae putative G protein, Gtr1p, which forms complexes with itself and a novel protein designated as Gtr2p, negatively regulates the Ran/Gsp1p G protein cycle through Gtr2p. Genetics 152, 853-867.
  • Kazuya Hara, et al. (1998) Archetype JC virus efficiently replicates in COS-7 cells, simian cells constitutively expressing simian virus 40 T antigen. Journal of Virology 72, 5335-5342.
  • Kaoru Kubokawa, Tomoyuki Miyashita and Yoshihiro Kubo. (1998) Isolation of a cDNA for a novel 120-kDa GTP-binding protein expressed in motor neurons in the salmon brain. Federation of European Biochemical Societies Letters 431, 231-235.
  • User Protocols

    Title
    TB320 KOD Polymerase