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J. Biol. Chem. 269, 30154-30157. Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity 1994

Pandey, A., Lazar, D.F., Saltiel, A.R. and Dixit, V.M.

Notes: [35S]methionine-labeled p85 regulatory subunit of PI 3-kinase was synthesized using the TNT® T7 Coupled Reticulocyte Lysate System. In GST-fusion assays, p85 bound to the native Eck cytoplasmic domain but not to the Eck deletion mutant that lacked the catalytic domain or to GST alone. (1808)

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Cell 79, 341-351. Adenovirus E1B 19kDa and Bcl-2 proteins interact with a common set of cellular proteins. 1994

Boyd, J.M., Malstrom, S., Subramanian, T., Venkatesh, L.K., Schaeper, U., Elangovan, B., D'Sa-Eipper, C. and Chinnadurai, G.

Notes: The yeast two-hybrid interaction cloning system was used to isolate cellular proteins that interact with E1B 19kDa protein. [35S]methionine-labeled proteins were expressed in vitro using the TNT® System and were then incubated with unlabeled cellular extracts. Anti-19kDa protein antibody was used for immunoprecipitation. Three proteins were found to interact with 19kDa protein. (errata in Cell, 79,1221.) (1760)

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Endocrinology 134, 998-1001. Agonists, but not antagonists, alter the conformation of the hormone-binding domain of androgen receptor. 1994

Kallio, P.J., Janne, O.A., Palvimo, J.J.

Notes: Wildtype and mutant androgen receptors (AR) were produced using the TNT® Coupled Reticulocyte Lysate System (in some reactions in the presence of [35S]methionine). In gel-retardation studies, the presence of agonists increases the mobility of AR-ARE complexes on nondenaturing gels. In partial proteolysis studies, agonists protect a 30kDa fragment from proteolysis. (0953)

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Mol. Cell. Biol. 14, 7816-7826. Analysis of the DNA-binding and dimerization activities of Neurospora crassa transcription factor NUC-1. 1994

Peleg, Y. and Metzenberg, R.L.

Notes: [35S]methionine-labeled NUC-1 proteins were expressed in the TNT® SP6 Coupled Reticulocyte Lysate System. Gel shift mobility assays were performed using the in vitro synthesized NUC-1 proteins and DNA from the pho-4+ gene. Wild type NUC-1 specifically interacts with the sequence tested. Following immunoprecipitation of NUC-1 proteins, chemical cross-linking was performed using the same DNA as before and indicates that NUC-1 forms homodimers. (1859)

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Clin. Exp. Immunol. 100, 205-213. Autoantigenic epitopes on eukaryotic L7. 1994

Von Mikecz, A., Hemmerich, P., Peter, H., Krawinkel, U.

Notes: The reactivity of antibodies from patients suffering from systemic autoimmune diseases was examined. Deletion mutants of recombinant L7 were expressed in the TNT® Coupled Reticulocyte Lysate System. Sera were collected from individuals suffering from systemic autoimmune diseases and were applied to immunoblots carrying total cell lysates. Immunoblots revealed that specific epitopes were often targets of antibodies in multiple patients, although the humoral autoimmune response and reactivity pattern of patient sera were heterogeneous. (1776)

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Parasitol. Res. 80, 478-486. Characterization of multiple unique cDNAs encoding the major surface glycoprotein of rat-derived Pneumocystis carinii. 1994

Linke, M.J., Smulian, A.G., Stringer, J.R., Walzer, P.D.

Notes: [35S]methionine-labeled protein was produced from the largest MSG cDNA clone and the viral gene 9 linked by a Factor Xa site using the TNT® Coupled Reticulocyte Lysate System. The product was digested with Factor Xa, and it was immunoprecipitated with MSG antibodies. There may be multiple MSG mRNAs that were transcribed, but it is not known if they are all translated. (0770)

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Biochim. Biophys. Acta 1219, 693-696. Cloning and characterization of a cDNA encoding rat PKR, the double-stranded RNA-dependent eukaryotic initiation factor-2 kinase. 1994

Mellor, H., Flowers, K.M., Kimball, S.R., Jefferson, L.S.

Notes: HCR (heme-controlled repressor) was produced using the TNT® Coupled Reticulocyte Lysate System and found to migrate on SDS-PAGE with an apparent mass of 85kDa instead of the predicted size of ~70kDa. The slower migration may be due to phosphorylation. (0677)

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J. Biol. Chem. 269, 21725-21734. Cloning and mutagenesis of the rabbit ApoB mRNA editing protein. A zinc motif is essential for catalytic activity, and noncatalytic auxiliary factor(s) of the editing complex are widely distributed. 1994

Yamanaka, S. , Poksay, K. S. , Balestra, M. E. , Zeng, G. Q. , Innerarity, T. L.

Notes: [35S]-labeled rabbit apoB mRNA editing protein (REPR) was generated using the TNT® Coupled Reticulocyte Lysate System. The protein was tested for mRNA editing of the apoB RNA substrate. The protein only edited the apoB mRNA when chicken enterocyte extract was added. (0134)

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Mol. Endocrinol. 8, 1434-1444. Cloning of a Novel Orphan Receptor (GCNF) Expressed during Germ Cell Development. 1994

Chen, F., Cooney, A.J., Wang, Y., Law, S.W. and O'Malley, B.W.

Notes: Mouse germ cell nuclear factor (mGCNF) was cloned from cDNA libraries. The hypothesized role for this protein is regulating gene expression during meiosis. mGCNF was synthesized using the TNT® T3 Coupled Reticulocyte Lysate System. Gel mobility analyses were performed with in vitro synthesized mGCNF in the absence and presence of labeled and cold DRO (direct repeats with 0 nucleotide spacing) and SF-1, HS and Oct-1 unlabeled nucleotides. GCNF can bind to an SF-1 half-site but not to an NBRE half-site. (1828)

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Genes Dev. 8, 576-586. Direct interaction of the U1 snRNP-A protein with the upstream efficiency element of the SV40 late polyadenylation signal. 1994

Lutz, C.S. and Alwine, J.C.

Notes: Full-length and fragments of [35S]methionine-labeled U1 snRNP-A protein were produced using the TNT® Coupled Reticulocyte Lysate System. The proteins were used in RNA-binding assays to the U1 RNA, SV40 RNA, pGEM® RNA (negative control) and triple mutant of SV40 sequences. The results show that the U1 snRNP-A is able to coprecipitate the U1 RNA and SV40 RNA, but a ten-fold reduction in precipitation of the triple mutant is seen. Both U1 fragments could bind the mutant but at greatly reduced levels. One U1 fragment precipitated both the U1RNA and the SV40 RNA; the other U1 fragment only precipitated the SV40 RNA. (1837)

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Science 264, 933-941. Drosophila TAFII150: similarity to yeast gene TSM-1 and specific binding to core promoter DNA. 1994

Verrijzer, C.P., Yokomori, K., Chen, J-.L. and Tjian, R.

Notes: Specific protein-protein interactions were mapped in vitro using a variety of techniques, including co-immunoprecipitation. dTAFII150DeltaN, dTAFII150DeltaC, pTAF150DeltaN and pTAF150DeltaC were expressed in the TNT® Coupled Reticulocyte Lysate System in the presence of 35S label. Protein A-Sepharose® beads were bound to antibodies to dTAFII250 or to the HA epitope and incubated with HA-dTBP, HA-dTAFII110 and dTAFII250DeltaN fusion proteins expressed in baculovirus. The 35S-labeled proteins were incubated with the antibody-baculovirus-expressed protein complexes and then analyzed by SDS-PAGE. dTAFII150 was shown to bind efficiently to immobilized HA-tagged dTBP and dTAFII250DeltaN, but did not interact selectively with dTAFII110 in vitro. (1775)

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J. Biol. Chem. 269, 25016-25020. Endothelial nitric oxide synthase membrane targeting. Evidence against involvement of a specific myristate receptor. 1994

Busconi, L. and Michels, T.

Notes: Wild type and mutant ecNOS (endothelial nitric oxide synthase) were synthesized in the TNT® Coupled Reticulocyte Lysate System in the presence of [3H]myristic acid. [3H] was incorporated into the wild type protein verifying that the in vitro synthesized protein undergoes myristolation. ecNOS was also synthesized in the presence of [35S]methionine and used in membrane association assays. ecNOS associates with the biological and denatured membranes. (1862)

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Cell 78, 617-624. Extradenticle raises the DNA binding specificity of homeotic selector gene products. 1994

Van Dijk, M.A. and Murre, C.

Notes: All proteins used in the study were synthesized using TNT® SP6 Coupled Reticulocyte Lysate System and were used for EMSAs. Extradenticle, a DNA binding partner of certain homeotic proteins, binds cooperatively with Ultrabithorax, Abdominal-A or Engrailed proteins to the oligonucleotide probe used in these studies. The Engrailed-Extradenticle binding site is distinct from that bound by Extradenticle-Ultrabithorax or Extradenticle-Abdominal-A. Extradenticle does not interact with Abdominal-B. (1834)

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Cell 79, 805-815. Groucho is required for Drosophila neurogenesis, segmentation, and sex determination and interacts directly with Hairy-related bHLH proteins. 1994

Paroush, Z., Finley, R.L. Jr., Kidd, T., Wainwright, S.M., Ingham, P.W., Brent, R. and Ish-Horowicz, D.

Notes: [35S]labeled Groucho protein was synthesized in vitro using the TNT® Coupled Reticulocyte Lysate System. The protein was incubated with GST, GST-hairy, GST-E(spl)-m7, GST-E(spl)-m8 and GST-T4 on glutathione beads. Gro interacts with all of the GST fusion proteins except GST-T4 (and the GST control). (1809)

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J. Virol. 68, 1728-1736. Identification and characterization of a protein kinase gene in the Lymantria dispar multinucleocapsid nuclear polyhedrosis virus. 1994

Bischoff, D.S. and Slavicek, J.M.

Notes: [35S]Methionine-labeled RalGDS (guanine nucleotide dissociation stimulator) was transcribed and translated in the TNT® T7 Coupled Reticulocyte Lysate System. The lysate was incubated with GTPase samples and used in immunoprecipitation assays with anti-RalGDS antisera. GST-R-ras, GST-H-ras and GST-Rap (Ras-like GTPases) bound with full length RalGDS in a GTP-dependent manner. In addition, Raf and RalGDS were shown to compete for binding to Ras-like GTPases. (1416)

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J. Biol. Chem. 269, 6842-6868. Identification of a novel retinoblastoma gene product binding site on human papillomavirus type 16 E7 protein. 1994

Patrick, D. R., Oliff, A., Heimbrook, D. C.

Notes: [35S]-methionine-labeled pRB60, pRB50 and pRB105 proteins were synthesized using TNT® Coupled Reticulocyte Lysate System. Experiments were performed with these proteins and GST fusion proteins to determine protein-binding sites. At low levels of GST-fusion protein, the pRB60 protein bound immobilized GST-E7(3-98) protein but did not bind the GST-E7-CR3 fusion or GST. The other truncated pRB translation products did not bind any GST constructs. With higher E7 concentrations, all pRB products bound the full length GST-E7 and CR3 domain fusion protein but did not bind GST. Complete binding was not observed, suggesting that denaturation, phosphorylation or other modifications render some fraction of these proteins unable to bind. The E7 CR2 and CR3 domains bind to non-overlapping domains on pRB. (0002)

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J. Biol. Chem. 269, 6842-6850. Identification of a novel retinoblastoma gene product-binding site on human papillomavirus type 16 E7 protein. 1994

Patrick, D.R., Oliff, A. and Heimbrook, D.C.

Notes: [35S]methionine-labeled pRB60, pRB50 and pRB105 proteins were synthesized using TNT® Coupled Reticulocyte Lysate System. Experiments were performed with these proteins and GST fusion proteins to determine protein-binding sites. At low levels of GST-fusion protein, the pRB60 protein bound immobilized GST-E7(3-98) protein but did not bind the GST-E7-CR3 fusion or GST. The other truncated pRB translation products did not bind any GST constructs. With higher E7 concentrations, all pRB products bound the full length GST-E7 and CR3 domain fusion protein but did not bind GST. Complete binding was not observed, suggesting that denaturation, phosphorylation or other modifications render some fraction of these proteins unable to bind. The E7 CR2 and CR3 domains bind to non-overlapping domains on pRB. (1810)

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Proc. Natl. Acad. Sci. USA 91, 12609-12613. Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap. 1994

Spaargaren, M. and Bischoff, J.

Notes: [35S]methionine-labeled RalGDS (guanine nucleotide dissociation stimulator) was transcribed and translated in the TNT® T7 Coupled Reticulocyte Lysate System. The lysate was incubated with GTPase samples and used in immunoprecipitation assays with anti-RalGDS antisera. GST-R-ras, GST-H-ras and GST-Rap (Ras-like GTPases) bind with full length RalGDS in a GTP-dependent manner. In addition, Raf and RalGDS compete for binding to Ras-like GTPases. (1814)

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Mol. Cell. Biol. 14, 3772-3781. Lipopolysaccharide induction of tissue factor gene expression in monocytic cells is mediated by binding of c-Rel/p65 heterodimers to a KB-like site. 1994

Oeth, P.A., Parry, G.C., Kunsch, C., Nantermet, P., Rosen, C.A. and Mackman, N.

Notes: p50, p65 and c-Rel (NF-kappaB/Rel proteins) were translated using the TNT® T7 Coupled Reticulocyte Lysate System. The proteins were checked for binding to NF-kappaB and Igkappa sites in electrophoretic mobility shift assays. p65 and c-Rel bind to TFkappaB-like sites, but neither p50/p65 heterodimers nor p50 homodimers bind to TFkappaB-like sites. p65, p65/p50 heterodimers and p50 homodimers all bind Igkappa but c-Rel does not bind Igkappa. (1843)

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Genes Dev. 8, 2756-2769. Multiple regions of TBP participate in the response to transcriptional activators in vivo. 1994

Tansey, W.P., Ruppert, S., Tjian, R. and Herr, W.

Notes: [35S]labeled TBPAS proteins were generated by in vitro transcription/translation using the TNT® Coupled Reticulocyte Lysate System. These proteins were incubated with hTAFII250 from S9 cells and whole cell extracts. In addition, TBPAS was incubated with GST-TFIIB: Approximately 10-fold more TBPAS was bound to the GST-TFIIB than to the GST alone. The results suggest that the recruitment of TBP into TFIID involves multiple interactions. (1783)

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Biochem. Soc. Trans. 22, 413S. Nuclear expression of mitochondrial genes implicated in human encephalomyopathies. 1994

Sutherland, L., Davidson, J., Jacobs, H. T.

Notes: This paper discusses the use of the TNT® Coupled Reticulocyte Lysate System to express mitochondrial genes in the mammalian cytosol and check for protein expression. (0324)

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Genomics 20, 1-4. Rapid detection of translation-terminating mutations at the adenomatous polyposis coli (APC) gene by direct protein truncation test. 1994

van der Luijt, R., Khan, P. M. , Vasen, H., van Leeuwen, C., Tops, C., Roest, P., den Dunnen, J., Fodde, R.

Notes: A 2kb fragment of the APC exon 15 (a mutation cluster region) was generated by PCR amplification from patient and tumor DNA. The PCR products were transcribed and translated in the TNT® T7 Coupled Reticulocyte Lysate System and subjected to the protein truncation test (PTT), the PTT revealed that several truncation mutations in exon 15 were responsible for different familial adenomatous polyposis cases. (0216)

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Virology 200, 413-427. Sequence analysis and expression of the murine cytomegalovirus phosphoprotein pp50, a homolog of the human cytomegalovirus UL44 gene product. 1994

Loh, L.C., Britt, W.J., Raggo, C. and Laferte, S.

Notes: [35S]methionine-labeled pp50 phosphoprotein was synthesized using the TNT® T7 Coupled Reticulocyte Lysate System. The protein was used in DNA-binding studies and shown to bind to both ssDNA-cellulose and dsDNA-cellulose but did not bind unmodified cellulose. The results suggest that pp50 may have a higher affinity for ssDNA than for dsDNA. (1858)

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EMBO J. 13, 5633-5638. The human Jkappa recombination signal sequence binding protein (RBP-Jkappa) targets the Epstein Barr Virus EBNA2 protein to its DNA responsive elements. 1994

Waltzer, L., Logeat, F., Brou, C., Israel, A., Sergeant, A. and Manet, E.

Notes: EBNA2 and RBP-Jkappa were produced using a TNT® System. RBP-Jkappa specifically binds to the Cp and Tp EBNA2-responsive elements. EBNA2 and RBP-Jkappa coimmunoprecipitate when translated together. Also, EBNA-RBP-Jkappa -DNA complexes form in vitro with Cp or Tp oligonucleotides. (1860)

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J. Biol. Chem. 269, 16909-16919. Topological analysis of H+, K+-ATPase using in vitro translation. 1994

Bamberg, K. and Sachs, G.

Notes: The membrane topology of the alpha subunit of the H+, K+-ATPase was investigated. DNA sequences encoding membrane-spanning segments were transcribed and translated using a troponin TNT® Coupled Reticulocyte Lysate System in the presence of [35S]methionine with and without microsomes. The data verify the first four and the eighth membrane-spanning segments of the alpha subunit. (2048)

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