Nucleotide Analogs - Jena Bioscience

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Sst I 5’...GAGCTC...3’ 3’...CTCGAG...5’ Cat. No. Size Conc. Price (€) EN-140S 1,600 units 10 u/µl 25,-- EN-140L 8,000 units 10 u/µl 100,-- Source: Streptomyces Stanford. Buffer supplied: 10x B1 and 10x BSA. Substrate for unit defi nition: λ DNA, Hind III digest (2 sites). Reaction conditions: 10 mM Tris-HCl (pH 7.9 @ 25°C), 10 mM MgCl , 1 mM dithiothreitol, 100 µg/ml 2 BSA. Incubate at 37°C. Storage buffer: 50 mM NaCl, 10 mM Tris-HCl (pH 7.4), 0.1 mM EDTA, 1 mM dithiothreitol, 200 µg/ml BSA and 50% glycerol. Store at -20°C. Ligation and recutting: After 10-fold overdigestion with Sst I, >95% of the DNA fragments can be ligated and recut with this enzyme. Heat inactivation: 65°C for 20 minutes. Sty I 5’...CCWWGG...3’ 3’...GGWWCC...5’ Cat. No. Size Conc. Price (€) EN-141S 6,000 units 10 u/µl 25,-- EN-141L 30,000 units 10 u/µl 100,-- Xba I 5’...TCTAGA...3’ 3’...AGATCT...5’ Cat. No. Size Conc. Price (€) EN-143S 3,500 units 10 u/µl 25,-- EN-143L 17,500 units 10 u/µl 100,-- Source: Xanthomonas badrii. Buffer supplied: 10x B2 and 10x BSA. Substrate for unit defi nition: λ DNA dam- Hind III digest (1 site). Reaction conditions: 50 mM NaCl, 10 mM Tris-HCl (pH 7.9 @ 25°C), 10 mM MgCl , 1 mM dithiothreitol, 2 100 µg/ml BSA. Incubate at 37°C. Storage buffer: 50 mM NaCl, 10 mM Tris-HCl (pH 7.4), 0.1 mM EDTA, 1 mM dithiothreitol, 200 µg/ml BSA and 50% glycerol. Store at -20°C. Ligation and recutting: After 50-fold overdigestion with Xba I, >98% of the DNA fragments can be ligated and recut with this enzyme. Star activity: Conditions of low ionic strength, high enzyme concentration or glycerol concentration >5% may result in star activity. Note: Blocked by overlapping dam methylation. Heat inactivation: 65°C for 20 minutes. Polymerases DNA Polymerase I Large Fragment (Klenow Fragment) Polymerases Cat. No. Amount Conc. Price (€) EN-148S 300 units 5 u/µl 25,-- EN-148L 1,500 units 5 u/µl 100,-- Source: Purifi ed from an E. coli strain carrying a DNA Polymerase I large fragment overproducing plasmid. Description: The Klenow Fragment lacks the 5’�3‘ exonuclease activity of intact DNA Polymerase I but retains the 5‘�3‘ polymerase, the 3‘�5‘ exonuclease and the strand displacement activities. Unit defi nition: One unit is defi ned as the amount of enzyme required to convert 10 nmoles of dNTPs to an acid insoluble form in 30 minutes at 37°C. Reaction conditions: 50 mM Tris-HCl (pH 7.6), 5 mM MgCl , 1 mM DTT and dNTPs (not included). Klenow 2 fragment is also 50% active in all fi ve standard <strong>Jena</strong> <strong>Bioscience</strong> buffers when supplemented with dNTPs. Storage buffer: 0.1 M KPO (pH 6.5), 1 mM DTT and 4 50% glycerol. Store: -20°C Heat inactivation: 75°C for 20 minutes. Fill-in conditions: Dissolve 0.1-4 µg of digested DNA in 1x reaction buffer supplemented with 40 µM each dNTP. Add 1 unit Klenow per µg DNA and incubate 15 minutes at 25°C. Stop the reaction by adding EDTA to 10 mM fi nal concentration and heating at 75°C for 10 minutes. Note: Excessive amounts of enzyme or longer reaction times may result in recessed ends due to the 3′�5′ exonuclease activity of the enzyme. Quality control: The enzyme is greater than 98% pure as indicated by SDS-polyacrylamide gel electrophoresis and contains no detected endonuclease activity. Incubation of 10 U of Klenow with supercoiled plasmid DNA produced no nicked molecules after 20 hours at 37°C as determined by agarose gel electrophoresis analysis. Source: E. coli WA921/pST27 hsd+. Buffer supplied: 10x B3 and 10x BSA. Substrate for unit defi nition: λ DNA (10 sites). Reaction conditions: 100 mM NaCl, 50 mM Tris-HCl (pH 7.9 @ 25°C), 10 mM MgCl , 1 mM dithiothreitol, 2 100 µg/ml BSA. Incubate at 37°C. Storage buffer: 50 mM KCl, 10 mM Tris-HCl (pH 7.4), 0.1 mM EDTA, 1 mM dithiothreitol, 200 µg/ml BSA and 50% glycerol. Store at -20°C. Ligation and recutting: After 10-fold overdigestion with Sty I, >98% of the DNA fragments can be ligated and recut with this enzyme. Heat inactivation: 65°C for 20 minutes. Taq I 5’...TCGA...3’ 3’...AGCT...5’ Cat. No. Size Conc. Price (€) EN-142S 4,500 units 10 u/µl 25,-- EN-142L 22,500 units 10 u/µl 100,-- Source: Thermus aquaticus YT I. Buffer supplied: 10x Taq I and 10x BSA. Substrate for unit defi nition: λ DNA dam- Klenow Fragment, 3’→5’ exo (121 sites). Reaction conditions: 100 mM KCl, 20 mM Tris-HCl (pH 8.5@ 25°C), 3 mM MgCl , 0,04% Triton X-100, 2 100 µg/ml BSA. Incubate at 65°C. Storage buffer: 300 mM KCl, 10 mM Tris-HCl (pH 7.4), 0.1 mM EDTA, 1 mM dithiothreitol, 500 µg/ml BSA and 50% glycerol. Store at -20°C. Ligation and recutting: After 10-fold overdigestion with Taq I, >90% of the DNA fragments can be ligated and recut with this enzyme. Note: Taq I is blocked by overlapping dam methylation. Incubation without BSA results in 50 % activity. Heat inactivation: 80°C for 20 minutes. - Recombinant, E. coli Cat. No. EN-151S EN-151L Amount 200 Units 1000 Units Price (€) 25,-- 100,-- Storage buffer: 100 mM KH PO /K HPO (pH 6.5), 2 4 2 4 1 mM DTT, and 50% glycerol. 1x Klenow Fragment Reaction Buffer: 10 mM Tris- HCl (pH 7.5), 5 mM MgCl , 7.5 mM DTT. 2 The Klenow Fragment is a proteolytic product of E. coli DNA Polymerase I that catalyzes the 5’�3‘ synthesis of DNA but has lost the 5‘�3‘ exonuclease activity. The exonuclease-defi cient variant is genetically engineered to abolish its 3‘�5‘ exonuclease activity. The enzyme is suited for second strand synthesis, particularly for synthesis of DNA using fl uorescent nucleotide analogs. Purity: > 95% by SDS-PAGE. Standard DNA Polymerase Assay Conditions: The polymerase activity is assayed in 1x Klenow Fragment reaction buffer including 300 µM dNTPs, M13mp18 ss-DNA, and M13 universal primer. Quantifi cation of ds-DNA is performed using PicoGreen ® DNA Polymerases Taq Pol Cat. No. Amount Price (€) PCR-201S 200 Units 35,-- PCR-201L 1000 Units Source: Thermus aquaticus strain YT 140,-- Description: Taq DNA Polymerase is a thermostable enzyme that catalyzes 5‘�3‘ synthesis of DNA. The enzyme has no detectable 3‘�5‘ proofreading exonuclease activity, but prossesses low 5‘�3‘ exonuclease activity. Quality Control Assays Standard DNA Polymerase Assay Conditions (not PCR conditions): The polymerase activity is assayed in 10 mM Tris-HCl (pH 8.5), 50 mM KCl, 1.5 mM MgCl , 200 µM each of dATP, dGTP, dCTP, dTTP (a 2 mix of unlabeled and [ . Absence of contaminants: Tested for the absence of endo- and exodeoxyribonucleases. Unit defi nition: One unit is defi ned as the amount of enzyme required to catalyze the incorporation of 10 nmoles of dNTPs into acid-insoluble material in 30 minutes at 37°C. Store: -20 °C 3H] dTTP) and 12.5 µg activated calf thymus DNA, in a fi nal volume of 50 µl. Functional Assay: Taq DNA Polymerase is tested for performance in the polymerase chain reaction (PCR) using 1.5 units of enzyme to amplify a 1730 bp region of the PspP I methyltransferase gene from 5 ng of bacterial genomic DNA. The resulting PCR product is visualized as a single band on an ethidium bromidestained agarose gel. Absence of contaminants: Tested extensively for the absence of endo- and exodeoxyribonucleases. Unit defi nition: One unit is defi ned as the amount of enzyme required to catalyze the incorporation of 10 nmoles of dNTPs into acid insoluble material in 30 minutes at 72°C. Taq DNA Polymerase Buffer (1x): 50 mM KCl, 10 mM Tris-HCl (pH 8.5), 1.5 mM MgCl , 0.1% Triton 2 X-100. Storage buffer: 100 mM NaCl, 50 mM Tris-HCl (pH 8.0), 1 mM DTT, 0.1 mM EDTA, 1% Triton X-100 and 50% glycerol. Store: -20oC Note: BSA is not included into the supplied reaction buffers and should be added separately from the supplied stock solution (1 mg/ml). * Requires Triton X-100 for optimal activity. TX-100 is included into the supplied reaction buffer. Enzymes 225
Enzymes 226 Selected references: Brakmann S. and Löbermann S. (2001) High-Density Labeling of DNA: Preparation and Characterization of the Target Material for Single-Molecule Sequencing. Angew. Chem. Int. Ed. 40: 1427. Tveit H. and Kristensen T. (2001) Fluorescence-based DNA polymerase assay. Anal. Biochem. 289:96. Sanger et al. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463. ® Pico Green dsDNA quantitation reagent is a trademark of Molecular Probes, Inc. RNA Polymerases RNA Pol II (RNA Polymerase II, native complex) human (HeLa cells), bovine (Calf Thymus) Cat. No. Amount Price (€) PR-713 2 µg 550,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. RNA Polymerase II is responsible for transcribing nuclear genes encoding the messenger RNAs and several small nuclear RNAs. It is composed of 12 subunits. The two largest subunits are the most highly conserved among eukaryotes and are homologous to the α- and β-subunits of the bacterial RNA Polymerase. RNA Pol II cannot recognize its target promoter directly and cannot initiate transcription without accessory factors. Instead, this large multisubunit enzyme relies on both general transcription factors and transcriptional activators and coactivators to regulate transcription from class II promoters. The carboxyl terminal domain (CTD) of RNA Polymerase II contains 52 repeats of a heptapeptide that has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery. Specifi c phosphorylation events at the CTD are associated with the spatial and temporal coordination of these different activities. Native RNA Polymerase II complex was purifi ed from HeLa cells nuclear pellet or calf thymus. RNA Polymerase II has been applied for in vitro transcription assays on naked as well as on chromatin templates and for protein-protein interactions assays. Unit defi nition: 1 unit equals 1 ng of purifi ed protein. 100 units are suffi cient for reconstituted in vitro transcription assay and 500 units are suffi cient for protein-protein interaction assay. Purity: > 95% by SDS-PAGE. Store: -80 °C Selected references: Woychik et al. (1994) R.C. Conaway and J.W. Conaway (eds), Raven Press NY: 227. Ossipow et al. (1995) A mammalian RNA polymerase II holoenzyme containing all components required for promoterspecifi c transcription initiation. Cell 83:137. Edwards et al. (1991) Two dissociable subunits of yeast RNA polymerase II stimulate the initiation of transcription at a promoter in vitro. J. Biol. Chem. 266:71. Flanagan et al. (1991) A mediator required for activation of RNA polymerase II transcription in vitro. Nature 350:436. Choy et al. (1993) Eukaryotic activators function during multiple steps of preinitiation complex assembly. Nature 366:531. Dahmus M.E. (1994) The role of multisite phosphorylation in the regulation of RNA polymerase II activity. Prog. Nucleic Acid Res. Mol. Biol. 48:143. Lu et al. (1991) The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex. Proc. Natl. Acad. Sci. USA 88:10004. O’Brien et al. (1994) Phosphorylation of RNA polymerase II Cterminal domain and transcriptional elongation. Nature 370:75. Lu et al. (1992) Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II. Nature 358:641. Cisek et al. (1989) Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2. Nature 339:679. Chambers et al. (1994) Purifi cation and characterization of a phosphatase from HeLa cells which dephosphorylates the Cterminal domain of RNA polymerase II. J. Biol. Chem. 269:26243. RNA Pol II-CTD (RNA Polymerase II, carboxy-terminal domain) human, Recombinant, E. coli Cat. No. Amount Price (€) PR-714 10 µg 350,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. The carboxy-terminal repeat domain (CTD) of the largest subunit of RNA Pol II contains tandem repeats of a heptapeptide sequence Tyr-Ser-Pro-Thr-Ser- Pro-Ser which is highly conserved among eukaryotic organisms. There are two forms of RNA Pol II in vivo, designated IIO, which is extensively phosphorylated at the CTD, and IIA, which is not phosphorylated. The IIA form preferentially enters the pre-initiation complex (PIC), whereas IIO is found in the elongating complex. The kinase activity of TFIIH can mediate CTD phosphorylation, although other kinases, including Cdc2, Ctk1, the Srb10-Srb11 kinase-cyclin pair, and P-TEFb, have also been implicated in CTD phosphorylation. A phosphatase responsible for the dephosphorylation of the CTD has also been identifi ed. CTD phosphatase activity is regulated by TFIIB and TFIIF. The CTD has also been implicated in pre-mRNA processing, most likely functioning as a platform for the recruitment and assembly of factors involved in pre-mRNA processing. Recombinant CTD is isolated from an E. coli strain that carries the coding sequence of human RNA Pol II carboxy-terminal domain under the control of a T7 promoter. CTD has been applied in in vitro transcription assays, splicing assays and protein-protein interactions assays. Protein is greater than 95% homogeneous and contains no detectable protease, DNase, and RNase activity. Unit defi nition: 1 unit equals 1 ng of purifi ed protein. 20 units are suffi cient for reconstituted transcription assay and 100 units are suffi cient for a protein-protein interaction assay. Purity: > 95% by SDS-PAGE. Store: -80 °C Selected references: Meinhart & Cramer (2004) Recognition of RNA polymerase II carboxy-terminal domain by 3’-RNA-processing factors. Nature 430:223 Lu et al. (1991) The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex. Proc. Natl. Acad. Sci. USA 88:10004. Dahmus M.E. (1994) The role of multisite phosphorylation in the regulation of RNA polymerase II activity. Prog. Nucleic Acid Res. Mol. Biol. 48:143. O’Brien et al. (1994) Phosphorylation of RNA polymerase II Cterminal domain and transcriptional elongation. Nature 370:75. Feaver et al. (1991) CTD kinase associated with yeast RNA polymerase II initiation factor b. Cell 67:1223. Cisek et al. (1989) Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2. Nature 339:679. Lee et al. (1991) CTD kinase large subunit is encoded by CTK1, a gene required for normal growth of Saccharomyces cerevisiae. Gene Expr. 1:149. Liao et al. (1995) A kinase-cyclin pair in the RNA polymerase II holoenzyme. Nature 374:193. Marshall et. al. (1996) Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271:27176. Chambers et al. (1994) Purifi cation and characterization of a phosphatase from HeLa cells which dephosphorylates the C-terminal domain of RNA polymerase II. J. Biol. Chem. 269: 26243. Chambers et al. (1995) The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB. J. Biol. Chem. 270:14962. McCracken et al. (1997) The C-terminal domain of RNA polymerase II couples mRNA processing to transcription. Nature 385:357. http://www.jenabioscience.com GST-CTD (RNA Polymerase II, Carboxyterminal Domain, GST-tagged) human, Recombinant, E. coli Cat. No. Amount Price (€) PR-796 10 µg 350,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. The carboxy-terminal repeat domain (CTD) of the largest subunit of RNA Pol II contains tandem repeats of a heptapeptide sequence Tyr-Ser-Pro-Thr-Ser- Pro-Ser which is highly conserved among eukaryotic organisms. There are two forms of RNA Pol II in vivo, designated IIO, which is extensively phosphorylated at the CTD, and IIA, which is not phosphorylated. The IIA form preferentially enters the pre-initiation complex (PIC), whereas IIO is found in the elongating complex. The kinase activity of TFIIH can mediate CTD phosphorylation, although other kinases, including Cdc2, Ctk1, the Srb10-Srb11 kinase-cyclin pair, and P-TEFβ, have also been implicated in CTD phosphorylation. A phosphatase responsible for the dephosphorylation of the CTD has also been identifi ed. CTD phosphatase activity is regulated by TFIIB and TFIIF. The CTD has also been implicated in pre-mRNA processing, most likely functioning as a platform for the recruitment and assembly of factors involved in pre-mRNA processing. Recombinant GST-CTD is isolated from an E. coli strain that carries the coding sequence of human RNA Pol II carboxy-terminal domain under the control of a T7 promoter. GST-CTD has been applied in protein-protein interactions assays. Protein is greater than 95% homogeneous and contains no detectable protease, DNase, and RNase activity. Unit defi nition: 100 units (ng) are suffi cient for a protein-protein interaction assay. Purity: > 95% by SDS-PAGE. Store: -80 °C Selected references: Meinhart & Cramer (2004) Recognition of RNA polymerase II carboxy-terminal domain by 3’-RNA-processing factors. Nature 430:223 Lu et al. (1991) The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex. Proc. Natl. Acad. Sci. USA 88:10004. Dahmus M.E. (1994) The role of multisite phosphorylation in the regulation of RNA polymerase II activity. Prog. Nucleic Acid Res. Mol. Biol. 48:143. O’Brien et al. (1994) Phosphorylation of RNA polymerase II Cterminal domain and transcriptional elongation. Nature 370:75. Feaver et al. (1991) CTD kinase associated with yeast RNA polymerase II initiation factor b. Cell 67:1223. Cisek et al. (1989) Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2. Nature 339:679. Lee et al. (1991) CTD kinase large subunit is encoded by CTK1, a gene required for normal growth of Saccharomyces cerevisiae. Gene Expr. 1:149. Liao et al. (1995) A kinase-cyclin pair in the RNA polymerase II holoenzyme. Nature 374:193. Marshall et. al. (1996) Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271:27176. Chambers et al. (1994) Purifi cation and characterization of a phosphatase from HeLa cells which dephosphorylates the C-terminal domain of RNA polymerase II. J. Biol. Chem. 269: 26243. Chambers et al. (1995) The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB. J. Biol. Chem. 270:14962. McCracken et al. (1997) The C-terminal domain of RNA polymerase II couples mRNA processing to transcription. Nature 385:357.
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JENA BIOSCIENCE Nucleotides and the
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2 Imprint: Design and Layout by: Gr
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Fax Order Form 4 Jena Bioscience Fa
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Terms/Conditions 6 General Business
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8 http://www.jenabioscience.com
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Nucleotide Analogs 10 General Infor
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Nucleotide Analogs 12 Fluorescent C
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Nucleotide Analogs 14 Labeled Amino
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Nucleotide Analogs 16 Labeled Cytid
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Nucleotide Analogs 18 Labeled γ-Am
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Nucleotide Analogs 20 Labeled with
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Nucleotide Analogs 26 Intrinsically
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Nucleotide Analogs 28 Selected refe
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Nucleotide Analogs 30 mant-GTPγS 2
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Nucleotide Analogs 32 http://www.je
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Nucleotide Analogs 34 Labeled Cytid
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Nucleotide Analogs 36 Labeled 8-[(4
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Nucleotide Analogs 38 Non-hydrolyza
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Nucleotide Analogs 40 dATPαS 2‘-
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Nucleotide Analogs 42 Selected refe
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Nucleotide Analogs 44 XTPγS Xantho
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Nucleotide Analogs 46 Bisubstrate I
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Nucleotide Analogs 48 Halogen conta
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Nucleotide Analogs 50 Hei et al. (1
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Nucleotide Analogs 52 Amine-labeled
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Nucleotide Analogs 54 Other Bases
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Nucleotide Analogs 56 dATPαS 2‘-
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Nucleotide Analogs 58 γ-Aminohexyl
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Nucleotide Analogs 60 Adenosine Nuc
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Nucleotide Analogs 62 d4TTP 2’,3
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Nucleotide Analogs 64 6-Thio-GTP 6-
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Nucleotide Analogs 66 Cyclic Nucleo
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Nucleotide Analogs 68 m 7 GTP 7-Met
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Nucleotide Analogs 70 XTP Xanthosin
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Nucleotide Analogs 72 Vial et al. (
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Nucleotide Analogs 74 Non-modifi ed
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Macromolecular Crystallography 78 C
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Macromolecular Crystallography 80 J
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Macromolecular Crystallography 94 W
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Macromolecular Crystallography 96 O
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Macromolecular Crystallography 100
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LEXSY 116 http://www.jenabioscience
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LEXSY 118 http://www.jenabioscience
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LEXSY 120 Secretory expression of t
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LEXSY 122 Synthetic serum- and prot
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LEXSY 124 Important licensing infor
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Recombinant Proteins 126 GTP Signal
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Recombinant Proteins 128 K-Ras 4B h
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Recombinant Proteins 130 Rab17 mous
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Recombinant Proteins 132 Selected r
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Recombinant Proteins 134 WASP-121 G
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Recombinant Proteins 136 G sαS -Le
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Recombinant Proteins 138 Store: -80
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Recombinant Proteins 140 Wenzel-Sei
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Recombinant Proteins 142 Mutation o
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Recombinant Proteins 144 Naunyn- Sc
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Recombinant Proteins 146 Protein co
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Recombinant Proteins 148 Membrane P
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Recombinant Proteins 150 TBP (TATA
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Recombinant Proteins 152 Store: -80
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Recombinant Proteins 154 RAP30 can
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Recombinant Proteins 156 and contai
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Recombinant Proteins 158 BRCA1 (Tum
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Recombinant Proteins 160 Unit defi
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Recombinant Proteins 162 p53, wild
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Recombinant Proteins 164 Sp1 (GC-bo
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Recombinant Proteins 166 p52 (Trans
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Recombinant Proteins 168 Topo I (Hu
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Recombinant Proteins 170 HMG1 (High
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Recombinant Proteins 172 Splicing F
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Page 177 and 178: Recombinant Proteins 176 GST-LXRα-
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Page 183 and 184: Recombinant Proteins 182 PI3 Kinase
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Page 213 and 214: Enzymes 212 Restriction Enzymes Res
Page 215 and 216: Enzymes 214 http://www.jenabioscien
Page 217 and 218: Enzymes 216 Restriction Enzymes Buf
Page 219 and 220: Enzymes 218 Relative Activity of Re
Page 221 and 222: Enzymes 220 Acc I 5’...GTMKAC...3
Page 223 and 224: Enzymes 222 EcoR V 5’...GATATC...
Page 225: Enzymes 224 Sca I 5’...AGTACT...3
Page 229 and 230: Enzymes 228 GST-RPB9 (RNA Polymeras
Page 231 and 232: Enzymes 230 T4 dNMP kinase Bacterio
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Page 237 and 238: Antibodies 236 Transcription Factor
Page 239 and 240: Antibodies 238 anti-Dr1 rabbit poly
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Page 245 and 246: PCR related Products 244 Standard P
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Page 271 and 272: Index 270 Product Catalog number Pa
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Index 276 Labeled γ-Aminooctyl-dUT
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Index 278 Constitutive LEXSY Starte
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Index 280 PrPc (full length, residu
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Index 282 dPTP, L pack ............
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Index 284 Catalog number Product Pa
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Index 286 CC-105 JBScreen Cryo 3 ..
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Index 288 NU-1014L NTP bundle (larg
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Index 290 NU-407S AppNHp (AMPPNP) .
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Index 292 NU-810-540Q Labeled EDA-A
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Index 294 NU-819L γ-Aminoethyl-App
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Index 296 PR-306 RCC1 (RanGEF) ....
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Nucleotide Analogs - Jena Bioscience

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