Nucleotide Analogs - Jena Bioscience

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assay; and 3) for cell growth and proliferation assays. Purifi ed protein is greater than 95% homogeneous and contains no detectable proteases, DNase, and RNase activity. Unit defi nition: 1 unit equals 1 ng of purifi ed protein. 1 unit is the amount suffi cient for a gel mobility shift assay in a 20 µl reaction. 50 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: Haber et al. (1991) Alternative splicing and genomic structure of the Wilms tumor gene WT1. Proc. Natl. Acad. Sci. USA 88: 9618. Haber et al. (1993) WT1-mediated growth suppression of Wilms tumor cells expressing a WT1 splicing variant. Science 262:2057. Kreidberg et al. (1993) WT-1 is required for early kidney development. Cell 74:679. Larsson et al. (1995) Subnuclear localization of WT1 in splicing or transcription factor domains is regulated by alternative splicing. Cell 81:391. Caricasole et al. (1996) RNA binding by the Wilms tumor suppressor zinc fi nger proteins. Proc. Natl. Acad. Sci. USA 93:7562. Little et al. (1997) A clinical overview of WT1 gene mutations. Hum. Mutat. 9:209. Englert et al. (1995) WT1 suppresses synthesis of the epidermal growth factor receptor and induces apoptosis. EMBO J. 14:4662. WT-1 (-KTS) (The Wilms’ Tumor Suppressor and Transcription/Pre-mRNA Splicing Factor) human, Recombinant, Sf9 insect cells Cat. No. Amount Price (€) PR-767 5 µg 450,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. WT-1, the product of Wilms’ Tumor suppressor gene Wt1, is a nuclear protein with structural motifs characteristic of transcription factors, including four C-terminal zinc fi ngers. While different pre-mRNA processing could result in 16 isoforms of the protein, inclusion or exclusion of exon 5 and the three amino acids (KTS) between zinc fi ngers 3 and 4 largely affects the activity of WT-1 protein. Such a complex post-transcriptional regulation, particularly in splicing, may represent a major regulatory mechanism for tumorigenesis of the Wilms’ tumor. WT1 (-KTS) appears to have different binding affi nity to both DNA and RNA comparing to the +KTS form. The WT-1 protein (residue 1-446, including exon 5 and without KTS) was expressed in baculovirus system and purifi ed by an affi nity column in combination with FPLC chromatography. Recombinant WT-1 protein can be used 1) for in vitro function studies including transcription, DNA or RNA binding assays; 2) for protein-protein interaction assay; and 3) for cell growth and proliferation assays. Purifi ed protein is greater than 95% homogeneous and contains no detectable proteases, DNase, and RNase activity. Unit defi nition: 1 unit equals 1 ng of purifi ed protein. 1 unit is suffi cient for a gel mobility shift assay in a 20 µl reaction. 50 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: Haber et al. (1991) Alternative splicing and genomic structure of the Wilms tumor gene WT1. Proc. Natl. Acad. Sci. USA 88: 9618. Haber et al. (1993) WT1-mediated growth suppression of Wilms tumor cells expressing a WT1 splicing variant. Science 262:2057. Kreidberg et al. (1993) WT-1 is required for early kidney development. Cell 74:679. Larsson et al. (1995) Subnuclear localization of WT1 in splicing or transcription factor domains is regulated by alternative splicing. Cell 81:391. Little et al. (1997) A clinical overview of WT1 gene mutations. Hum. Mutat. 9:209. Englert et al. (1995) WT1 suppresses synthesis of the epidermal growth factor receptor and induces apoptosis. EMBO J. 14:4662. Co-activators Transcriptional activators and co-activators regulate gene expression and numerous stagespecifi c functions during cell cycling. Their specifi city for the target promoter/enhancer is determined by the DNA-binding domain which can be a I) zinc fi nger motif (loop of ~23 amino acids), II) homeodomain (~60 amino acids with 3 α-helices), III) helix-loop-helix motif (40-50 amino acids with 2 α-helices separated by a loop), or IV) a leucine zipper (amphipatic helix that dimerizes). BRG1 (Brahma-related Gene 1 Protein, wild type) human, Recombinant, Sf9 insect cells Cat. No. Amount Price (€) PR-740 5 µg 450,-- Liquid. Supplied as a 0.25 mg/ml solution in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. The wild type human brahma-related gene 1 (Brg1) encodes a protein of 1,647 amino acids that contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription regulation. BRG1 is an essential component of the SWI/SNF chromatin remodeling complexes and implicated in multiple functions through its interaction with different proteins, including the tumor suppressor protein pRb, serine-threonine kinase LKB1, and other transcription factors. Although Brg1 involves in chromatin remodeling as complexes with other SWI/SNF proteins, purifi ed BRG1 itself is capable of remodeling mono-nucleosomes and nucleosomal arrays in vitro. Mutations of Brg1 have been found in multiple tumor cell lines. The wild type human BRG1 was expressed in baculovirus system and purifi ed by an affi nity column in combination with FPLC chromatography. Recombinant BRG1 can be used 1) for protein-protein interaction assay; 2) for in vitro transcription assay; 3) for in vitro nucleosome remodeling assay; and 4) for cell growth assay. Purifi ed protein is greater than 95% homogeneous and contains no detectable proteases, DNase, and RNase activity. Unit defi nition: 50-100 units (ng) are required for in vitro nucleosome remodeling assay and 100 units are required for a protein-protein interaction assay. Purity: > 95% by SDS-PAGE. Store: -80 °C Selected references: Khavari et al. (1993) BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription. Nature 366:170. Fryer C.J. and Archer T.K. (1998) Chromatin remodelling by Transcription Factors the glucocorticoid receptor requires the BRG1 complex. Nature 393:88. Sif et al. (1998) Mitotic inactivation of a human SWI/SNF chromatin remodeling complex. Genes Dev. 12:2842. Dunaief et al. (1994) The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest. Cell 79:119. Marignani et al. (2001) LKB1 associates with Brg1 and is necessary for Brg1-induced growth arrest. J. Biol. Chem. 276: 32415. Brockmann et al. (2001) The histone acetyltransferase activity of PCAF cooperates with the brahma/SWI2-related protein BRG-1 in the activation of the enhancer A of the MHC class I promoter. Gene 277:111. Barker et al. (2001) The chromatin remodelling factor Brg-1 interacts with beta-catenin to promote target gene activation. EMBO J. 20:4935. Phelan et al. (1999) Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits. Mol. Cell 3:247. Wong et al. (2000) BRG1, a component of the SWI-SNF complex, is mutated in multiple human tumor cell lines. Cancer Res. 60:6171. BRG1-mt K798R (Brahma-related Gene 1 Protein) human, Recombinant, Sf9 insect cells Cat. No. Amount Price (€) PR-741 5 µg 400,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. BRG1 is an essential component of the SWI/SNF chromatin remodeling complexes and implicated in multiple functions through its interaction with different proteins, including the tumor suppressor protein pRb, serine-threonine kinase LKB1, and other transcription factors. Mutation of lysine to arginine at position 798 in the DNA-dependent ATPase domain of BRG1 a) failed to restore normal growth to swi2-cells, b) reduced its ability to repress c-fos transcription, and c) reduced CIITA (class II transactivator) induction and enhanced the rate of induction of the interferon-γ-responsive GBP-1 gene. The mutant human BRG1 (K798R) was expressed in baculovirus system and purifi ed by an affi nity column in combination with FPLC chromatography. Recombinant BRG1 (K798R) can be used 1) for protein-protein interaction assay; 2) for in vitro transcription assay; 3) for in vitro nucleosome remodeling assay; and 4) for cell growth assay. Purifi ed protein is greater than 95% homogeneous and contains no detectable proteases, DNase, and RNase activity. Unit defi nition: 100 units (ng) are required for a protein-protein interaction assay. Purity: > 95% by SDS-PAGE. Store: -80 °C Selected references: Dunaief et al. (1994) The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest. Cell 79:119. Marignani et al. (2001) LKB1 associates with Brg1 and is necessary for Brg1-induced growth arrest. J. Biol. Chem. 276: 32415. Brockmann et al. (2001) The histone acetyltransferase activity of PCAF cooperates with the brahma/SWI2-related protein BRG-1 in the activation of the enhancer A of the MHC class I promoter. Gene 277:111. Barker et al. (2001) The chromatin remodelling factor Brg-1 interacts with beta-catenin to promote target gene activation. EMBO J. 20:4935. Khavari et al. (1993) BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for normal mitotic growth and transcription. Nature 366:170. Murphy et al. (1999) Human SWI-SNF component BRG1 represses transcription of the c-fos gene. Mol. Cell. Biol. 19: 2724. Pattenden et al. (2002) Interferon-gamma-induced chromatin remodeling at the CIITA locus is BRG1 dependent. EMBO J. 21:1978. Recombinant Proteins 165
Recombinant Proteins 166 p52 (Transcriptional Coactivator) human, Recombinant, E. coli Cat. No. Amount Price (€) PR-728 10 µg 400,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. The human p52 protein is a non-TAF transcription coactivator that mediates activator-dependent transcription by RNA Polymerase II. The function of p52 is through interactions with transcriptional activators and the basal transcription machinery. In addition, p52 could also interact with several cellular proteins including the transcription coactivator PC4, the essential splicing factor ASF/SF2 and the nuclear protein nucleolin. Recombinant p52 protein (wild type, 333 amino acids) is isolated from an E. coli strain that carries the coding sequence of human p52 under the control of T7 promoter and purifi ed by the combination of an affi nity column and FPLC chromatography. Recombinant p52 has been utilized for in vitro function studies, including transcription, splicing, protein-DNA/ RNA and protein-protein interactions. 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. 1 unit is suffi cient for a gel mobility shift assay in a 20 µl reaction; 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: Ge et al. (1998) Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation. EMBO J. 17:6723. Ge et al. (1998) A novel transcriptional coactivator, p52, functionally interacts with the essential splicing factor ASF/SF2. Molecular Cell 2:751. Ge, H. (2000) UPA, a universal protein array system for quantitative detection of protein-protein, protein-DNA, protein- RNA and protein-ligand interactions. Nucleic Acid Res. 28:e3. p75 (Transcriptional Coactivator and Lens Epithelial Cell- Derived Growth Factor) human, Recombinant, E. coli Cat. No. Amount Price (€) PR-729 10 µg 400,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. The human p75 protein, similar to p52, is a non-TAF transcription coactivator that mediates activatordependent transcription by RNA Polymerase II in vitro through most tested activators. Although p75 and p52 are derived from alternatively splicing of a single gene and share most coding sequence, they reveal different function in several aspects. In addition to functioning as a transcription coactivator, p75 has been shown to be involved in growth of epithelial cells as a lens epithelial cell-derived growth factor (LEDGF), and in pathogenesis of atopic dermatitis as an autoantigen. Recombinant p75 protein (wild type, 530 amino acids) is isolated from an E. coli strain that carries the coding sequence of human p75 under the control of T7 promoter and purifi ed by an affi nity column in combination with FPLC chromatography. Recombinant p75 has been utilized for in vitro function studies, including transcription, splicing, protein-DNA/ RNA and protein-protein interactions. 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. 1 unit is suffi cient for a gel mobility shift assay in a 20 µl reaction; 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: Ge et al. (1998) Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation. EMBO J. 17:6723. Ge et al. (1998) A novel transcriptional coactivator, p52, functionally interacts with the essential splicing factor ASF/SF2. Molecular Cell 2:751. Singh et al. (2000) Lens epithelium-derived growth factor (LEDGF/p75) and p52 are derived from a single gene by alternative splicing. Gene 242:265. Singh et al. (1999) Lens epithelium-derived growth factor: increased resistance to thermal and oxidative stresses. Invest Ophthalmol Vis. Sci. 40:1444. Ochs et al. (2000) Autoantibodies to DFS 70 kd/transcription coactivator p75 in atopic dermatitis and other conditions. J. Allergy Clin. Immunol. 105:1211. p75-CTR [C-terminal region of p75 (LEDGF)] human, Recombinant, E. coli Cat. No. Amount Price (€) PR-758 10 µg 400,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. Lens Epithelium-derived Growth Factor (LEDGF, also called as p75) has been shown to enhance survival of lens epithelial cells (LECs) against stress. LEDGF is a transcriptional activator. It protects the cells by binding to cis-stress response ((A/T)GGGG(T/A)), and heat shock (HSE; nGAAn) elements in the stress genes and activating their transcription. Originally, it was isolated as a co-activator required for transcriptional activation in human cell-free systems containing RNA Polymerase II and general initiation factors. LEDGF is expressed at all stages of development in a variety of organs and tissues. A second protein product, p52, can be produced from the same gene due to alternative splicing of pre-mRNA. In vitro, p52 was found to be more general and stronger transcriptional co-activator than LEDGF/p75. HIV-1 integrase (IN) forms a specifi c nuclear complex with p75 but not with p52, suggesting a role for p75’s C-terminal region in retroviral integration. Recombinant p75 CTR is isolated from an E. coli strain that carries the C-terminal coding sequence of the human LEDGF/p75 (amino acid 322-530) under the control of a T7 promoter. p75 has been applied in in vitro transcription assays, splicing assays, DNA and protein-protein interaction assays. The purifi ed recombinant protein is greater than 95% homogeneous and contains no detectable protease, DNase, and RNase activity. Unit defi nition: 20 units (ng) are suffi cient for an in vitro transcription assay and 100 units are suffi cient for a protein-protein interaction assay. Purity: > 95% by SDS-PAGE. Store: -80 °C Selected references: Fatma et al. (2001) Transcriptional regulation of the antioxidant protein 2 gene, a thiol-specifi c antioxidant, by lens epitheliumderived growth factor to protect cells from oxidative stress. J. Biol. Chem. 276:48899. http://www.jenabioscience.com Singh et. al. (2001) LEDGF binds to heat shock and stressrelated element to activate the expression of stress-related genes. Biochem. Biophys. Res. Commun. 283:943. Ge et al. (1998) Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation. EMBO J. 17:6723. Maertens et al. (2003) LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells. J. Biol. Chem. 278:33528. p300 (Tumor Suppressor Protein and Transcription Factor) human, Recombinant, Sf9 insect cells Cat. No. Amount Price (€) PR-762 2 µg 450,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol. Human p300 and CBP (CREB Binding Protein) are highly related transcriptional coactivators. Both proteins have been identifi ed through protein interaction assays. In addition to interacting with variety of cellular factors and onco-proteins, loss of the wild type CBP alleles in isolated tumors suggests that CBP/p300 might serve as tumor suppressors. The ability of p300 to acetylate many transcription factors, including p53, E2F, TFIIE, and TFIIF etc. demonstrated a novel mechanism of targeted p300 regulation of gene expression. The wild type p300 (2414 amino acid residues) was expressed in baculovirus system and purifi ed by an affi nity column in combination with FPLC chromatography. Recombinant p300 can be used 1) for protein-protein interaction assay; 2) for in vitro transcription assay; 3) for in vitro acetylation assay; and 4) for cell growth assay. Purifi ed protein is greater than 95% homogeneous and contains no detectable proteases, DNase, and RNase activity. Unit defi nition: 1 unit equals 1 ng of purifi ed protein. 1 unit is suffi cient for a gel mobility shift assay in a 20 µl reaction; 50 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: Stein et al. (1990) Analysis of E1A-mediated growth regulation functions: binding of the 300-kilodalton cellular product correlates with E1A enhancer repression function and DNA synthesis-inducing activity. J. Virol. 64:4421. Eckner et al. (1994) Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes & Dev. 8:869. Kung et al. (2000) Gene dose-dependent control of hematopoiesis and hematologic tumor suppression by CBP. Genes & Dev. 14:272. Imhof et al. (1997) Acetylation of general transcription factors by histone acetyltransferases. Curr. Biol. 7:689. Gu et al. (1997) Activation of p53 sequence-specifi c DNA binding by acetylation of the p53 C-terminal domain. Cell 90:595. Martinez-Balbas et al. (2000) Regulation of E2F1 activity by acetylation. EMBO J. 19:662. p300 (C1135-2414) (p300 C-terminus, HAT Domain) human, Recombinant, Sf9 insect cells Cat. No. Amount Price (€) PR-770 4 µg 450,-- Liquid. Supplied in 20 mM Tris-HCl, pH 7.9, 100 mM KCl, 0.2 mM EDTA, 1 mM DTT, 20% glycerol.
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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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Page 127 and 128: Recombinant Proteins 126 GTP Signal
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Page 139 and 140: Recombinant Proteins 138 Store: -80
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Page 163 and 164: Recombinant Proteins 162 p53, wild
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Page 173 and 174: 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
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Enzymes 216 Restriction Enzymes Buf
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Enzymes 218 Relative Activity of Re
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Enzymes 220 Acc I 5’...GTMKAC...3
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Enzymes 222 EcoR V 5’...GATATC...
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Enzymes 224 Sca I 5’...AGTACT...3
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Enzymes 226 Selected references: Br
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Enzymes 228 GST-RPB9 (RNA Polymeras
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Enzymes 230 T4 dNMP kinase Bacterio
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Enzymes 232 Topo I Core (Human DNA
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Antibodies 236 Transcription Factor
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Antibodies 238 anti-Dr1 rabbit poly
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Antibodies 240 PI3 Kinase Antibodie
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PCR related Products 244 Standard P
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PCR related Products 246 DNA Mutage
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PCR related Products 248 Polymerase
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PCR related Products 250 Primers an
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PCR related Products 252 DNA Sequen
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PCR related Products 254 50 bp DNA
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Affi nity Chromatography 256 Immobi
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Affi nity Chromatography 260 γ-Ami
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Affi nity Chromatography 264 γ-Ami
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Affi nity Chromatography 268 2’/3
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Index 270 Product Catalog number Pa
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Index 272 Labeled 5-Propargylamino-
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Index 274 Labeled EDA-ATP + 5-FAM..
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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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