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Promega Corporation

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J. Cell Sci. 117, 2937-49. Carbohydrates act as sorting determinants in ER-associated degradation of tryosinase. 2004

Svedine, S., Wang, T., Halaban, R. and Herbert, D.N.

Notes: Wildtype and albino mutant tyrosinase were translated in Rabbit Reticulocyte Lysate, Nuclease Treated, supplemented with canine microsomal membranes or semipermeabilized melanocytes. After translation, SP-melanocytes were isolated and resuspended in Rabbit Reticulocyte Lysate, Untreated, in the presence of an ATP regenerating system, and ER-associated degradation of the proteins was evaluated. (3375)

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Microbiology 145, 999-1004. Proteolytic cleavage of the A subunit is essential for maximal cytotoxicity of Eschericia coli O157:H7 Shiga-like toxin-1. 1999

Lea, N., Lord, J.M., Roberts, L.M.

Notes: Rabbit Reticulocyte Lysate, Untreated, was used a source of ribosomes for the assay of Shiga-like toxin-1 to depurinate 28S rRNA. No details of how the ribosomes were purified are provided. (0850)

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J. Biol. Chem. 274, 403-407. The carboxyl terminus of interferon-γ contains a functional polybasic nuclear localization sequence. 1999

Subramaniam, P.S., Mujtaba, M.G., Paddy, M.R., Johnson, H.M.

Notes: The authors used Rabbit Reticulocyte Lysate, Untreated, in an in vitro nuclear transport assay with permeabilized mouse A31 cells grown on coverslips. (0308)

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J. Biol. Chem. 273, 22745-22752. The cAMP-dependent protein kinase site (Ser312) enhances dorsal nuclear import through facilitating nuclear localization sequence/importin interaction. 1998

Briggs, L.J., Stein, D., Goltz, J., Corrigan, V.C., Efthymiadis, A., Hübner, S., Jans, D.A.

Notes: Promega's Untreated Rabbit Reticulocyte Lysate was used to reconstitute nuclear localization signal-dependent nuclear import into mechanically perforated HTC rat hepatoma cells. The import required the lysate, an energy generating system consisting of creatine phosphokinase, creatine phosphate and ATP. The nuclear import of a fluorescein-tagged protein was followed by confocal laser scanning microscopy. (1404)

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EMBO J. 16, 2703-2716. Cell-free synthesis and assembly of connexins into functional gap junction membrane channels. 1997

Falk, M.M., Buehler, L.K., Kumar, N.M. and Gilula, N.B.

Notes: Several different gap junction channel subunit isotypes, also known as connexins, were synthesized in vitro in the presence of Canine Microsomal Membranes. Translation reactions were spun through a sucrose cushion to separate the membrane fraction from the supernatant. Connexins that integrated into the microsomes formed homo- and heterooligomeric structures. The assembled proteins in the microsome were fused with a synthetic membrane and single channel conductance was measured and found to be very similar to wild-type membranes. (1618)

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J. Biol. Chem. 272, 6119-6127. Topological rules for membrane protein assembly in eukaryotic cells. 1997

Gafvelin, G., Sakaguchi, M., Andersson, H. and von Heijne, G.

Notes: The paper looked at the insertion of a model protein with one, two and four transmembrane segments and different distributions of positively charged residues in the N-terminal tail and the polar loops. The proteins were translated in the presence of the microsomes. Translocation of polypeptides to the lumenal side of the microsomes was assayed by prevention of N-linked glycosylation through competitive inhibition by the addition of a glycosylation acceptor tripeptide but not by a nonacceptor tripeptide and by proteinase K treatment of the microsomes. All techniques are referenced. (2033)

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Proc. Natl. Acad. Sci. USA 93, 15497-15502. Molecular recognition of pathogen attack occurs inside of plant cells in plant disease resistance specified by the Arabidopsis genes RPS2 and RPM1. 1996

Leister, R.T., Ausubel, F.M., Katagiri, F.

Notes: The RSP2 protein was in vitro translated using Promega's Rabbit Reticulocyte Lysate in the presence of microsomes. The protein was not protected from proteinase K digestion and deemed to be a cytoplasmic protein. (1626)

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J. Biol. Chem. 271, 24151-24156. Mutual transcriptional interference between RelA and androgen receptor. 1996

Palvimo, J. J. , Reinikainen, P. , Ikonen, T. , Kallio, P. J. , Moilanen, A. , Janne, O. A.

Notes: Native and mutated AR cDNAs were transcribed with the TNT® T7 Coupled Reticulocyte Lysate System. The reaction mixtures were divided and supplemented with either androgen or vehicle. For EMSAs, the preincubated receptors were placed in binding reactions with [32P]-labeled dsDNA corresponding to a glucocorticoid/androgen-responsive element (ARE). All AR receptors with intact DNA-binding domains formed specific complexes with the ARE. The presence of active hormone altered the mobility of receptor-DNA complexes probably due to a conformational change. Mutant proteins could form heterodimers with native AR that interacted with DNA. Androgen receptor (AR) was translated using the Rabbit Reticulocyte Lysate System, and RelA was translated using Wheat Germ Extract. Coimmunoprecipitation was performed with anti-AR or anti-RelA, but no specific association between AR and RelA was detected (even with the cross-linking agent dithiobis(succinimidylpropionate) present). This finding does not exclude the possibility that AR-RelA interactions occur in vivo. (1669)

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J. Biol. Chem. 271(47), 29928-29936. The Dri 42 gene, whose expression is up-regulated during epithelial differentiation, encodes a novel endoplasmic reticulum residuent transmembrane protein. 1996

Barilá, D., Plateroti, M., Nobili, F., Muda, A.O., Xie, Y., Morimoto, T. and Perozzi, G.

Notes: The protein with six membrane-spanning domains was translated using Rabbit Reticulocyte Lysate in the presence of Canine Microsomal Membranes. The protein was N-glycosylated and this glycosylation was sensitive to endoglycosidase H. Mutants containing one to all six transmembrane domain were constructed and immunoprecipitates tested for susceptibility to protease digestion and determination of membrane topology. The full protein could only be inserted cotranslationally since incubation of translation products with puromycin and the membranes produced no protection from the proteases. (1648)

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Biochem. J. 317, 195-202. Type-III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disulphide bonds but triple-helix nucleation does require hydroxylation. 1996

Bulleid, N.J., Wilson, R. and Lees, J.F. .

Notes: RNA coding for a type-III procollagen mini-gene was translated in the Rabbit Reticulocyte Lysate System in the absence of DTT. The polypeptides produced were treated with NEM and immunoprecipitated with antibodies specific for type-III procollagen and separated with or without reduction. Translation products from mutants were digested with chymotrypsin, trypsin and pepsin in the presence and absence of alpha, alpha´-dipyridyl to determine if a correctly aligned triple helix had formed in the mutants. (1761)

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Hum. Mol. Genet. 4, 1989-1991. Detection of BRCA1 mutations by the protein truncation test. 1995

Plummer, S. J., Anton Culver, H., Webster, L., Noble, B., Liao, S., Kennedy, A., Belinson, J., Casey, G.

Notes: The Protein Truncation Test (PTT) is investigated as a rapid, first mutation screening approach in exon 11 of the BRCA1 gene. Eighty-one percent of the mutations found in 63 patients are truncation mutations, and 49% of these mutations are in exon 11 so the PTT is a sound screening method. The Wheat Germ Extract performed better than the Rabbit Reticulocyte Lysates with the primer set used. The investigators suggest that the choice of translation be empirically determined for each primer set used. (0538)

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