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Mol. Cell. Biol. 15, 4507-4517. A 10 amino-acid sequence in the N-Terminal A/B domain of thyroid hormone receptor alpha is essential for transcriptional activation and interaction with the general transcription factor TFIIB. 1995

Hadzic, E., Desai-Yajnik, V., Helmer, E., Guo, S., Wu, S., Koudinova, N., Casanova, J., Raaka, B.M. and Samuels, H.H.

Notes: The thyroid hormone receptor-alpha was tested for interaction of its A/B domain with TFIIB. The labeled proteins were prepared using the TNT® Coupled Reticulocyte Lysate System with L-[35S]cysteine or L-[35S]methionine. The labeled proteins were incubated with GST-TFIIB and shown to interact in vitro. (1796)

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EMBO J. 14, 5589-5596. A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. 1995

Chittenden, T., Flemington, C., Houghton, A.B., Ebb, R.G., Gallo, G.J., Elangovan, B., Chinnadurai, G. and Lutz, R.J.

Notes: [35S]methionine-labeled HA-Bak and HA-BakDeltaGD were synthesized in vitro using the TNT® Coupled Reticulocyte Lysate System. These proteins were used in interaction assays with GST-Bcl-xL to detect interactions between regions of Bak and Bcl-xL. (1790)

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Nucl. Acids Res. 23, 2076-2077. A rapid method to deplete endogenous DNA-binding proteins from reticulocyte lysate translation systems. 1995

Ebel, T. and Sippel, A.

Notes: Biotinylated dsDNA containing the NFI binding site was incubated with the TNT® Coupled Reticulocyte Lysate System. Streptavidin-coated beads were added, and the DNA-protein complexes and beads were removed through magnetic fractionation. The supernatant was then used as the lysate without endogenous DNA-binding proteins present. (1823)

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Science 269, 1580-1583. A VAMP-binding protein from aplysia required for neurotransmitter release. 1995

Skehel, P.A., Martin, K.C., Kandel, E.R. and Bartsch, D.

Notes: V. californica VAMP was translated in vitro using the TNT® T7 Coupled System. It bound VAP-33 and GST-syntaxin fusion protein specifically. This result suggests that additional factors may not be required for binding to occur. (1812)

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Cancer Res. 55, 501-504. Acceleration of apoptosis in transforming growth factor beta 1-treated M1 cells ectopically expressing B-myb. 1995

Bies, J. and Wolff, L.

Notes: [35S]Cysteine-labeled beta-myb was synthesized using the TNT® T3 Coupled Reticulocyte Lysate System. The protein was the approximate size predicted from the cDNA. (1449)

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Nature 377, 362-365. Activation of a cell-cycle-regulated histone gene by the oncogenic transcription factor IRF-2. 1995

Vaughan, P.S., Aziz, F., van Wijnen, A.J., Wu, S., Harada, H., Taniguchi, T., Soprano, K.J., Stein, J.L. and Stein, G.S.

Notes: IRF-1 and IRF-2 (interferon (IFN) regulatory factors 1 and 2), the positive and negative regulators of IFN-beta transcription, were produced using the TNT® Coupled Reticulocyte Lysate System. The proteins were analyzed in EMSAs with wild type and mutant CCE (cell-cycle element) probe. Both IRF-1 and IRF-2 bind CCE specifically. (1819)

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Mol. Endocrinol. 9, 1441-1454. Analysis of transcription and estrogen insensitivity in the female mouse after targeted disruption of the estrogen receptor gene. 1995

Couse, J. F. , Curtis, S. W. , Washburn, T. F. , Lindzey, J. , Golding, T. S. , Lubahn, D. B. , Smithies, O. , Korach, K. S.

Notes: Estrogen receptor knockout mice (ERKO) were created in previous work. Estrogen receptor (ER) from the ERKO line was in vitro translated using the TNT® Coupled Reticulocyte Lysate System using [35S]labeled methionine. The ERKO mice have a smaller ER that has reduced estrogen-dependent transcriptional activity compared to wild type. (1283)

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Cell 83, 979-992. Aplysia CREB2 represses long-term facilitation: Relief of repression converts transient facilitation into long-term functional and structural change. 1995

Bartsch, D., Ghirardi, M., Skehel, P.A., Karl, K.A., Herder, S.P., Chen, M., Bailey, C.H. and Kandel, E.R.

Notes: [35S]methionine-labeled ApCREB2 and ApC/EBP were translated in the TNT® Coupled Reticulocyte Lysate System. In vitro interaction assays were performed with the labeled ApCREB2 and ApC/EBP and with GST fusions of ApCREB2 and its deletion mutants. ApCREB2 forms weak homodimers, and ApCREB2 interacts with ApC/EBP. (1781)

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Genes Dev. 9, 995-1008. Assembly and function of a TCRalpha enhancer complex is dependent on LEF-1-induced DNA bending and multiple protein-protein interactions. 1995

Giese, K., Kingsley, C., Kirshner, J.R. and Grosschedl, R.

Notes: [35S]methionine-labeled Ets-1 was synthesized in vitro using the TNT® Coupled Reticulocyte Lysate System. In vitro translated [35S]labeled Ets-1 was incubated with immobilized ATF-2194 on nitrocellulose membranes and with GST-ATF-2194 on glutathione-agarose beads, and the proteins were shown to associate. (1793)

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FEBS Lett. 357, 168-172. Autoprocessing of HSV-1 protease: effect of deletions on autoproteolysis. 1995

Godefroy, S., Guenet, C.

Notes: The HSV-1 protease UL26-encoded protein was produced using the TNT® Coupled Reticulocyte Lysate System. The N-terminal autoproteolysis of UL26 protein was shown in vitro and was abolished when residues 245-248 were deleted. The autoproteolysis of this protease may be achieved in a defined order. (1107)

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Oncogene 11, 1921-1928. Bik, a novel death-inducing protein shares a distinct sequence motif with Bcl-2 family proteins and interacts with viral and cellular survival-promoting proteins. 1995

Boyd, J.M., Gallo, G.J., Elangovan, B., Houghton, A.B., Malstrom, S., Avery, B.J., Ebb, R.G., Subramanian, T., Chittenden, T., Lutz, R.J., et al.

Notes: Bik was identified, cloned, and characterized. Bik contains a short sequence with homology to Bax and Bak that may be sufficient for protein interaction. [35S]methionine-labeled proteins were expressed in vitro using the TNT® Coupled Reticulocyte Lysate System. The Bik, Bax, and Bak proteins were tested for interaction with GST-Bcl-2, GST-Bcl-xL or GST. Bik interacts with Bcl-2 and Bcl-xL in vitro. (1750)

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J. Virol. 69, 6323-6334. Bovine papillomavirus Type 1 E2 transcriptional regulators directly bind two cellular transcription factors, TFIID and TFIIB. 1995

Rank, N.M. and Lambert, P.F.

Notes: RBP and TFIIB were synthesized using the TNT® Coupled Reticulocyte Lysate System and Trans[35S]label (ICN). These proteins were used in in vitro protein association assays in the presence of DNA containing E2 and TBP binding sites. Cooperative DNA binding by E2 and TBP is mediated by the direct binding of E2 to TBP. (1832)

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J. Biol. Chem. 270, 17488-17493. cAMP response element-binding protein (CREB) interacts with transcription factors IIB and IID. 1995

Xing, L., Gopal, V.K. and Quinn, P.G.

Notes: [35S]labeled CREB or mutated CREB proteins were synthesized in the in vitro TNT® Coupled Reticulocyte Lysate System. These proteins were mixed with ETFIIB and coimmunoprecipitated with anti-T7 Tag epitope mAb. (1780)

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J. Cell Sci. 108, 675-683. CDEBP, a site-specific DNA-binding protein of the 'APP-like' family, is required during the early development of the mouse. 1995

Blangy, A., Vidal, F., Cuzin, F., Yang, Y.H., Boulukos, K. and Rassoulzadegan, M.

Notes: CDEBP was synthesized using the TNT® T7 Coupled Reticulocyte Lysate System. [35S]-labeled protein was analyzed by SDS-PAGE and immunoprecipitated with anti-CDEBP polyclonal antibody. The unlabeled protein was shown to bind the CDEI motif in gel shift assays (EMSA). (2043)

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Gene 162, 297-302. cDNA cloning and characterization of the transcriptional activities of the hamster peroxisome proliferator-activated receptor haPPAR gamma. 1995

Aperlo, C., Pognonec, P., Saladin, R., Auwerx, J. and Boulukos, K. E.

Notes: The cDNA clone of haPPARγ was transcribed and translated in the TNT® Coupled Reticulocyte Lysate System. The protein product was labeled with [35S]methionine and used in electrophoretic mobility shift assays (EMSAs) with [32P]labeled dsDNA probe. The probe used was the PPRE (peroxisome proliferator response element) from the acyl-CoA oxidase promoter. The haPPARγ effectively bound PPRE. (1479)

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Anal. Biochem. 232, 31-36. Cell-free synthesis of functional type IV adenylyl cyclase. 1995

Warner, D., Basi, N.S. and Rebois, R.V.

Notes: The cDNA for type IV adenylyl cyclase (ACIV) was expressed in the TNT® Coupled Reticulocyte Lysate System in the presence of [35S]methionine. Adenylyl cyclase activity was assayed, and the protein was immunoprecipitated with antibodies to ACIV. The adenylyl cyclase was activated by bovine brain Gs and forskolin and was quite stable. This report showed that ACIV can be produced in vitro with the activity of baculovirus-produced ACIV. (1777)

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Biochem. J. 308, 673-681. Chimeric constructs show that the unique N-terminal domain of the cyclic AMP phosphodiesterase RD1 (RNPDE4A1A; rPDE-IVA1) can confer membrane association upon the normally cytosolic protein chloramphenicol acetyltransferase. 1995

Scotland, G., Houslay, M.D.

Notes: Different RD1-CAT [35S]methionine-labeled chimeric proteins were produced using the TNT® Coupled Reticulocyte Lysate System. The chimeric proteins showed that the unique N-terminal domain of RD1 confers membrane association upon the cytosolic CAT protein. (0419)

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J. Virol. 69, 6209-6218. Chimeric proteins composed of Jun and CREB define domains required for interaction with the human T-cell leukemia virus type 1 Tax Protein. 1995

Yin, M.J., Paulssen, E., Seeler, J. and Gaynor, R.B.

Notes: [35S]methionine-labeled wild type and mutant CREB proteins and CREB-Jun chimeras were synthesized using the TNT® T7 Coupled Reticulocyte Lysate System. The dimerization of these proteins was analyzed in vitro. CREB proteins with double mutations in the leucine zipper region were unable to interact with Tax whereas CREB proteins with only single mutations in the region or wild type CREB proteins were able to dimerize with Tax. (GST analyses were performed with bacterial expressed proteins.) (1789)

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J. Biol. Chem. 270, 18715-18718. Cleavage of poly(ADP-ribose) polymerase by interleukin-1beta converting enzyme and its homologs TX and Nedd-2. 1995

Gu, Y., Sarnecki, C., Aldape, R.A., Livingston, D.J. and Su, M.S.

Notes: [35S]methionine-labeled pre-IL-1beta and PARP(T) proteins were synthesized using the TNT® T7 Coupled Reticulocyte Lysate System and were used for cleavage studies. The proteins were incubated with purified recombinant human ICE, which cleaved both proteins. The cleavage of PARP requires 50- to 100-fold higher concentrations of ICE than required for pre-IL-1beta cleavage. (1904)

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Oncogene 11, 131-139. Discordant regulation of SCL/TAL-1 mRNA and protein during erythroid differentiation. 1995

Murrell, A.M., Bockamp, E.O., Gottgens, B., Chan, Y.S., Cross, M.A., Heyworth, C.M., Green, A.R.

Notes: [35S]methionine-labeled SCL (HLH transcription factor) and LYL-1 (a related bHLH protein) were produced using the TNT® T7 Coupled Reticulocyte Lysate System. The proteins were run on SDS-PAGE before and after immunoprecipitation with anti-SCL antiserum. The anti-SCL immunoprecipitated the SCL protein but not the LYL-1 protein. (0633)

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J. Biol. Chem. 270, 14666-14671. Elt-2, a second GATA factor from the nematode Caenorhabditis elegans. 1995

Hawkins, M.G. and McGhee, J.D.

Notes: ELT-2 protein was produced using the TNT® System. The DNA binding activity was analyzed by gel mobility shift assays using the putative gut activator region of the C. elegans ges-1 gene. The protein binds the GATA sequences of the gene and is competed effectively with unlabeled oligo, except when those GATA sequences in the competitor are mutated to GTCGCC. (1802)

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Cell 81, 505-512. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. 1995

Chinnaiyan, A. M. , O'Rourke, K. , Tewari, M. , Dixit, V. M.

Notes: A yeast 2-hybrid interaction cloning system was used to isolate the novel interacting protein, FADD, which interacts with the cytoplasmic domain of Fas. Labeled FADD was prepared in vitro using the TNT® T7 Coupled Reticulocyte Lysate System and used to demonstrate that the death domains of FADD and GST-Fas interact. (1187)

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Mech. Dev. 52, 99-108. Hox gene products modulate the DNA binding activity of Pbx1 and Pbx2. 1995

Van Dijk, M., Peltenburg, L.T.C., and Murre, C.

Notes: Pbx1, Pbx2, Hoxb-8, Hoxb-7, and Engrailed-2/Pbx1 fusion proteins were produced in the TNT® SP6 Coupled Reticulocyte Lysate System. In vitro translated proteins were analyzed by EMSA using various DNA fragments. Hoxb-8 modulates the DNA binding activity of Pbx1 and Pbx2; Pbx1 and Hoxb-8 bind to DNA as heterodimers; Pbx1 and Pbx2 bind to DNA cooperatively with Hoxb-7. (1818)

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J. Virol. 69, 2850-2857. Human adenovirus serotypes 3 and 5 bind to two different cellular receptors via the fiber head domain. 1995

Stevenson, S.C., Rollence, M., White, B., Weaver, L. and McClelland, A.

Notes: Human adenovirus serotypes 3 and 5 were expressed in vitro using the TNT® T7 Coupled Reticulocyte Lysate System and were labeled with [35S]methionine. The proteins were then analyzed by SDS-PAGE and fluorography and by binding to HeLa cell monolayers followed by SDS-PAGE. The trimeric forms of the proteins were the only forms able to bind to the cells. Other work shows that the proteins bind different cellular receptors. (1788)

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Genes Dev. 9, 2747-2755. Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation. 1995

Ruppert, S. and Tjian, R.

Notes: C-terminal truncated RAP74 proteins were synthesized in the TNT® Coupled Reticulocyte Lysate System. These truncated mutants were used in coimmunoprecipitation assays with HA-hTAFII250. The recognition interfaces between the proteins were mapped using these assays. (1774)

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