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71085 | KOD DNA Polymerase

71085
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      Número de referenciaDisponiblidad Embalaje Cant./Env. Precio Cantidad
      US171085-3
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          Frasco de vidrio 250 u
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          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.
          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

          Documentation

          Ficha datos de seguridad (MSDS)

          Título

          Ficha técnica de seguridad del material (MSDS) 

          Certificados de análisis

          CargoNúmero de lote
          71085

          Referencias bibliográficas

          Visión general referencias
          Nishioka, M., et al. 2001. J. Biotechnol. 88, 141. Takagi, M., et al. 1997. Appl. Environ. Microbiol. 63, 4504.

          Folleto

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          PCR Protocols and Guides - Simplify your gene discovery (MM)

          Citas

          Título
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        • 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.
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        • 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.
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