Nucleotide Analogs - Jena Bioscience

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anti-TFIIH (anti-p62) rabbit polyclonal antibody Cat. No. Amount Price (€) ABD-007 50 µg 400,-- Liquid. Supplied in PBS. TFIIH, a multisubunit complex is involved in several biological fundamental mechanisms of the cell: transcription, nucleotide excision repair and cell cycle regulation. p62 is one of the six subunits that constitutes the core of TFIIH. Analysis of the expression of the p62 gene reveals an over-expression in testis tissue. This subunit of TFIIH participates in a variety of protein-protein interactions. For example, Rb competes with TBP and p62 for binding to E2F thus repressing E2F-mediated transactivation; herpes simplex virus VP16 and human p53, directly interact with the p62 subunit of TFIIH. In addition, TFIIH, via p62 phosphorylation is the major target for mitotic inactivation of transcription. α-TFIIH is an affi nity-purifi ed rabbit polyclonal antibody raised against a recombinant full-length p62 protein. Specifi city α-TFIIH reacts with the p62 protein in HeLa nuclear extract (cat.# PR-777) by Western blotting. Recommended dilution range for Western blot analysis: 1:200 - 1:1000. Store: -20 °C Selected references: Feaver et al. (1991) Purifi cation and characterization of yeast RNA polymerase II transcription factor b. J. Biol. Chem. 266: 19000. Flores et al. (1992) Factors involved in specifi c transcription by mammalian RNA polymerase II. Identifi cation and characterization of factor IIH. J. Biol. Chem. 267:2786. Fischer et al. (1992) Cloning of the 62-kilodalton component of basic transcription factor BTF2. Science 257:1392. Perez et al. (1998) Genomic organization and promoter characterization of the mouse and human genes encoding p62 subunit of the transcription/DNA repair factor TFIIH. Gene 213:73. Pearson A. and Greenblatt J. (1997) Modular organization of the E2F1 activation domain and its interaction with general transcription factors TBP and TFIIH. Oncogene 15:2643. Xiao et al. (1994) Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53. Mol Cell Biol. 14:7013. Long et al. (1998) Repression of TFIIH transcriptional activity and TFIIH-associated cdk7 kinase activity at mitosis. Mol Cell Biol. 18:1467. anti-RNA Pol II (anti-CTD) mouse monoclonal antibody (ascites) Cat. No. Amount Price (€) ABD-008 125 µl 400,-- Liquid. Supplied as ascites. 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. α-RNA Pol II (CTD) is a mouse monoclonal antibody (ascites) without further purifi cation. Specifi city α-RNA Pol II (CTD) reacts with the CTD subunit in HeLa nuclear extract (cat.# PR-777) by Western blotting. Recommended dilution range for Western blot analysis: 1:2000 - 1:5000. Store: -20 °C Selected references: 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. anti-RNA Pol II (anti-p33) rabbit polyclonal antibody Cat. No. Amount Price (€) ABD-009 50 µg 400,-- Liquid. Supplied in PBS. hRPB5 (p33) is a highly conserved subunit shared by all three RNA Polymerases. It has been shown to be in close contact to promoter DNA when Pol II is recruited into the preinitiation complex. RPB5 has also been implicated in direct protein-protein contacts with Transcription Factor IIB, RAP30 subunit of Transcription Factor IIF, and gene-specifi c modulator proteins, such as the hepatitis B virus transactivator protein X or an inhibitor of Pol II, RMP (RPB5mediating protein). Therefore, RPB5 is facilitating the communication between the Pol II core and a variety of basal and gene-specifi c transcription factors. In the Pol II complex, RPB5 interacts with RPB3 and the RPB3–RPB5 interaction is intensifi ed in the presence of three subunits, RPB7, RPB8 and RPB11. RPB5 also makes direct contacts with both RPB1 and RPB2, the two large subunits of the polymerase complex. α-RNA Pol II (p33) is an affi nity-purifi ed rabbit polyclonal antibody raised against a recombinant fulllength p33 subunit of the polymerase complex. Specifi city α-RNA Pol II (p33) reacts with the p33 protein in HeLa nuclear extract (cat.# PR-777) by Western blotting. Recommended dilution range for Western blot analysis: 1:200 - 1:1000. Store: -20 °C Selected references: Woychik et al. (1990) Subunits shared by eukaryotic nuclear RNA polymerases. Genes Dev. 4:313. Kim et al. (1997) Trajectory of DNA in the RNA polymerase II transcription preinitiation complex. Proc. Natl. Acad. Sci. USA 94:12268. Lin et al. (1997) Hepatitis B virus X protein is a transcriptional modulator that communicates with transcription factor IIB and Antibodies the RNA polymerase II subunit 5. J. Biol. Chem. 272:7132. Wei et al. (2001) Direct interaction between the subunit RAP30 of transcription factor IIF (TFIIF) and RNA polymerase subunit 5, which contributes to the association between TFIIF and RNA polymerase II. J. Biol. Chem. 276:12266. Dorjsuren et al. (1998) RMP, a novel RNA polymerase II subunit 5-interacting protein, counteracts transactivation by hepatitis B virus X protein. Mol. Cell. Biol. 18:7546. Miyao et al. (1996) Molecular assembly of RNA polymerase II from the fi ssion yeast Schizosaccharomyces pombe: subunitsubunit contact network involving Rpb5. Genes Cells 1:843. Kimura et al. (2000) Involvement of multiple subunit-subunit contacts in the assembly of RNA polymerase II. Nucleic Acids Res. 15:952. anti-RNA Pol II (anti-p14.5) rabbit polyclonal antibody Cat. No. Amount Price (€) ABD-010 50 µg 400,-- Liquid. Supplied in PBS. hRPB9 is a subunit unique to RNA Polymerase II, although it has sequence homologues in RNA Polymerases I and III. The gene for Rpb9 is not essential for yeast cell viability, but is essential in Drosophila. hRPB9 has roles in both transcription initiation and transcription elongation. In the initiation reaction it is necessary for accurate start site selection. In the elongation reaction, RPB9, along with TFIIS facilitates the conversion of an arrestcompetent conformation to a read-through competent conformation. RNA Polymerase II lacking the RPB9 subunit uses alternate transcription initiation sites in vitro and in vivo and is unable to respond to the transcription elongation factor TFIIS in vitro. A role in the modulation of initiation and elongation is consistent with the localization of RPB9 in the threedimensional structure of yeast RNA Polymerase II. RPB9 is located at the tip of the so-called “jaws” of the enzyme, which is thought to function by clamping the DNA downstream of the active site. RPB9 comprises two zinc ribbon domains joined by a conserved linker region. The C-terminal zinc ribbon is similar in sequence to that found in TFIIS. α-RNA Pol II (p14.5) is an affi nity-purifi ed rabbit polyclonal antibody raised against a recombinant fulllength p14.5 subunit of the polymerase complex. Specifi city α-RNA Pol II (p14.5) reacts with the p14.5 subunit in HeLa nuclear extract (cat.# PR-777) by Western blotting. Recommended dilution range for Western blot analysis: 1:200 - 1:1000. Store: -20 °C Selected references: Woychik et al. (1991) Yeast RNA polymerase II subunit RPB9 is essential for growth at temperature extremes. J. Biol. Chem. 266:19053. Nogi et al. (1993) Gene RRN4 in Saccharomyces cerevisiae encodes the A12.2 subunit of RNA polymerase I and is essential only at high temperatures. Mol. Cell. Biol. 13:114. Harrison et al. (1992) The RNA polymerase II 15-kilodalton subunit is essential for viability in Drosophila melanogaster. Mol. Cell. Biol. 12:928. Furter-Graves (1991) SHI, a new yeast gene affecting the spacing between TATA and transcription initiation sites. Mol. Cell. Biol. 11:4121. Awrey (1997) Transcription elongation through DNA arrest sites. A multistep process involving both RNA polymerase II subunit RPB9 and TFIIS. J. Biol. Chem. 272:14747. Hemming et al. (2000) RNA polymerase II subunit Rpb9 regulates transcription elongation in vivo. J. Biol. Chem. 275: 35506. Cramer et al. (2000) Architecture of RNA polymerase II and implications for the transcription mechanism. Science 288:640. Qian (1993) Structure of a new nucleic-acid-binding motif in eukaryotic transcriptional elongation factor TFIIS. Nature 365: 277. Antibodies 237
Antibodies 238 anti-Dr1 rabbit polyclonal antibody Cat. No. Amount Price (€) ABD-011 50 µg 400,-- Liquid. Supplied in PBS. Dr1 is a general negative regulator of class II and class III gene expression. It binds to the basic repeat domain of TBP on promoter DNA and can prevent the RNA Polymerase II holoenzyme, or its TFIIB and/or TFIIA subunits, from assembling into an initiation complex. Dr1 is phosphorylated in vivo and this modifi cation affects its interaction with TBP. In addition, Dr1 interacts with the hyperphosphorylated form of Pol II and with the repression domain of the AREB6 repressor. Dr1 forms a heterodimer complex with DRAP1 through its histone fold domain. More recently it was discovered that Dr1-DRAP1 is a bi-functional basal transcription factor that differentially regulates gene transcription through DPE (downstream promoter elements) or TATA box motifs. It can stimulate transcription in vitro from Drosophila promoters containing DPEs, whereas it represses transcription from TATA-containing promoters. α-Dr1 is an affi nity-purifi ed rabbit polyclonal antibody raised against a recombinant full-length Dr1 protein. Specifi city α-Dr1 reacts with the Dr1 protein in HeLa nuclear extract (cat.# PR-777) by Western blotting. Recommended dilution range for Western blot analysis: 1:200 - 1:1000. Store: -20 °C Selected references: Inostroza et al. (1992) Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription. Cell 70:477. White et al. (1994) Differential regulation of RNA polymerases I, II, and III by the TBP-binding repressor Dr1. Science 266:448. Mermelstein et al. (1996) Requirement of a corepressor for Dr1mediated repression of transcription. Genes Dev. 10:1033. Kim et al. (1995) TATA-binding protein residues implicated in a functional interplay between negative cofactor NC2 (Dr1) and general factors TFIIA and TFIIB. J. Biol. Chem. 270:10976. Castano et al. (2000) The C-terminal domain-phosphorylated IIO form of RNA polymerase II is associated with the transcription repressor NC2 (Dr1/DRAP1) and is required for transcription activation in human nuclear extracts. Proc. Natl. Acad. Sci. USA 97:7184. Ikeda et al. (1998) Involvement of negative cofactor NC2 in active repression by zinc fi nger-homeodomain transcription factor AREB6. Mol. Cell. Biol. 18:10. Goppelt et al. (1996) A mechanism for repression of class II gene transcription through specifi c binding of NC2 to TBPpromoter complexes via heterodimeric histone fold domains. EMBO J. 15:3105. Willy et al. (2000) A basal transcription factor that activates or represses transcription. Science 290:982. anti-HMG1 rabbit polyclonal antibody Cat. No. Amount Price (€) ABD-012 50 µg 400,-- Liquid. Supplied in PBS. High mobility group 1 (HMG1) is a 26 kDa highly conserved non-sequence-specifi c DNA-binding nuclear protein. Mammalian HMG1 has two homologous DNA-binding domains HMG boxes, A and B (each of 80–90 amino-acid residues), linked by a short basic region to an acidic C-terminal domain containing 30 consecutive Asp and Glu residues. HMG1 has been implicated in a number of fundamental biological processes including transcription, replication and recombination, in which it plays a role in manipulating DNA structure by bending, looping, compaction or unwinding, or by direct contacts with distinct cellular proteins. HMG1 can act as a repressor, by interacting with TBP to block pre-initiation complex formation or as an activator, by facilitating the binding of various transcription factors to their cognate DNA sequences. Most recently, it was discovered that HMG1 is a late mediator of delayed endotoxin lethality by activating downstream cytokine release. α-HMG1 is an affi nity-purifi ed rabbit polyclonal antibody raised against a recombinant full-length HMG1 protein. Specifi city α-HMG1 reacts with the HMG1 protein in HeLa nuclear extract (cat.# PR-777) by Western blotting. Recommended dilution range for Western blot analysis: 1:200 - 1:1000. Store: -20 °C Selected references: Bianchi et al. (1989) Specifi c recognition of cruciform DNA by nuclear protein HMG1. Science 243:1056. Bustin et al. (1990) Structural features of the HMG chromosomal proteins and their genes. Biochim. Biophys. Acta 1049:231. Zappavigna et al. (1996) HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation. EMBO J. 15:4981. Zlatanova et al. (1998) Binding to four-way junction DNA: a common property of architectural proteins? FASEB J. 12:421. Stelzer et al. (1994) Repression of basal transcription by HMG2 is counteracted by TFIIH-associated factors in an ATPdependent process. Mol. Cell. Biol. 14:4712. Lu et al. (2000) Infl uence of HMG-1 and adenovirus oncoprotein E1A on early stages of transcriptional preinitiation complex assembly. J. Biol. Chem. 275(45):35006. Jayaraman et al. (1998) High mobility group protein-1 (HMG-1) is a unique activator of p53. Genes Dev. 12:462. Onate et al. (1994) The DNA-bending protein HMG-1 enhances progesterone receptor binding to its target DNA sequences. Mol. Cell. Biol. 14:3376. Yang et al. (2001) HMG-1 rediscovered as a cytokine. Shock 15:247. anti-DNA Topoisomerase I rabbit polyclonal antibody Cat. No. Amount Price (€) ABD-013 50 µg 400,-- Liquid. Supplied in PBS. Human DNA Topoisomerase I (Topo I) is a monomeric protein of 765 amino acids encoded by a single-copy gene. Based on its function, DNA Topoisomerase I has been subdivided into four distinct domains. The N-terminal 214 amino acids of Topo I comprise a highly charged N-terminal domain involved in protein-protein interactions with a number of cellular proteins. The highly conserved core domain expanded from amino acids 215 to 636 contains most catalytic residues and retains DNA binding activity. The active C-terminal domain (residues 713-765) is connected to the core domain by a poorly conserved linker domain (residues 636-712). Human DNA Topoisomerase I is the best studied of the DNA Topoisomerase family. It catalyzes the relaxation of both positive and negative supercoiled DNAs without the requirement of energy. In addition to DNA replication and transcriptional activation, DNA Topoisomerase I also plays a major role in pre-mRNA splicing, cell cycle and other gene regulatory pathways during cell growth and development. Since Topo I can cause large amounts of single-strand DNA breaks and this kind of DNA damage closely relates to most cancer, it is therefore believed that DNA Topo I can be an important target for antitumor agents. α-Topo I is an affi nity-purifi ed rabbit polyclonal antibody raised against a recombinant full-length DNA Topoisomerase I protein. Specifi city α-Topo I reacts with the DNA Topoisomerase I protein in HeLa nuclear extract (cat.# PR-777) by Western blotting. Recommended dilution range for Western blot analysis: 1:200 - 1:1000. Store: -20 °C http://www.jenabioscience.com Selected references: Liu et al. (1981) Eukaryotic DNA topoisomerases: two forms of type I DNA topoisomerases from HeLa cell nuclei. Proc. Natl. Acad. Sci. USA 78 :3487. Juan et al. (1988) Human DNA topoisomerase I is encoded by a single-copy gene that maps to chromosome region 20q12-13.2. Proc. Natl. Acad. Sci. USA 85:8910. Stewart et al. (1996) Biochemical and biophysical analyses of recombinant forms of human topoisomerase I. J. Biol. Chem. 271:7593. Stewart et al. (1996) The domain organization of human topoisomerase I. J. Biol. Chem. 271:7602. Redinbo et al. (1998) Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. Science 279:1504. Pourquier et al. (1997) Trapping of mammalian topoisomerase I and recombinations induced by damaged DNA containing nicks or gaps. Importance of DNA end phosphorylation and camptothecin effects. J. Biol. Chem. 272:26441. Sekiguchi et al. (1996) Resolution of Holliday junctions by eukaryotic DNA topoisomerase I. Proc. Natl. Acad. Sci. USA 93:785. Kretzschmar et al. (1993) Identifi cation of human DNA topoisomerase I as a cofactor for activator-dependent transcription by RNA polymerase II. Proc. Natl. Acad. Sci. USA 90:11508. Rossi et al. (1996) Specifi c phosphorylation of SR proteins by mammalian DNA topoisomerase I. Nature 381:80. Giovanella et al. (1989) DNA topoisomerase I--targeted chemotherapy of human colon cancer in xenografts. Science 246:1046. Pommier et al. (1998) Mechanism of action of eukaryotic DNA topoisomerase I and drugs targeted to the enzyme. Biochem. Biophys. Acta 1400:83. anti-RXR (anti-RXR-LBD) rabbit polyclonal antibody Cat. No. Amount Price (€) ABD-014 50 µg 400,-- Liquid. Supplied in PBS. Retinoid X receptor (RXR) serves as a promiscuous heterodimerization partner for many nuclear receptors through the identity box, a 40-amino acid subregion within the ligand binding domain (LBD). RXR partners include thyroid hormone receptors (TRs), retinoic acid receptors (RARs), peroxisome proliferatoractivated receptor, several constitutive active orphan nuclear receptors (e.g. nuclear growth factor I-B), oxysterol receptors, and constitutive androstane receptors. RXRs also form homodimers to mediate the effects of 9-cis-retinoic acid (9-cRA). Depending on these protein-protein interactions, RXR-containing complexes have distinct ligand-dependent and constitutive functions. The LBD is functionally complex and mediates ligand binding, receptor homo- and heterodimerization, repression of transcription in the absence of ligand, and ligand-dependent activation of transcription. Hormone binding to the structurally conserved LBD of the RXR triggers a conformational change that principally affects the conserved C-terminal transactivation helix H12 involved in transcriptional activation. α-RXR is an affi nity-purifi ed rabbit polyclonal antibody raised against the recombinant ligand-binding domain of the RXR protein. Specifi city α-RXR reacts with the RXR protein in HeLa nuclear extract (cat.# PR-777) by Western blotting. Recommended dilution range for Western blot analysis: 1:200 - 1:1000. Store: -20 °C Selected references: Mangelsdorf et al. (1995) The nuclear receptor superfamily: the second decade. Cell 83:835. Nakashima et al. (1999) Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300. Science 284:479. Egea et al. (2001) Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR. J. Mol. Biol. 307:557.
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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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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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Recombinant Proteins 174 Lim-Tio et
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Recombinant Proteins 176 GST-LXRα-
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Recombinant Proteins 178 Unit defi
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Recombinant Proteins 180 Purity: >
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Recombinant Proteins 182 PI3 Kinase
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Recombinant Proteins 184 Selected r
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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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