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Citations Search

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J. Neuroendocrinol. 19, 309-319. Inhibition of vasopressin V1b receptor translation by upstream open reading frames in the 5'-untranslated region. 2007

Rabadan-Diehl, C., Martínez, A., Volpi, S., Subburaju, S. and Aguilera, G.

Notes: The authors studied the rat VP V1b receptor (V1bR) gene including the 826 base 5´ UTR, which has five ORFs upstream (uORF) of the V1bR protein start codon, to examine the effect of the upstream peptides on V1bR translation. The V1bR gene was cloned into the pALTER®-MAX Vector, and substitution mutations were created in the uORF translation initiation codons with the Altered Sites® II in vitro Mutagenesis System. One microgram of the linearized pALTER®- V1bR construct was transcribed using the Riboprobe® System and translated using Wheat Germ Extract with or without 35S-methionine. The unlabeled protein was analyzed by Western blot. The radiolabeled protein was spun through a 3% sucrose cushion, precipitated and separated by SDS-PAGE. For a possible membrane-targeted protein, the uORF1 was transcribed in vitro and then translated using Rabbit Reticulocyte Lysate, Canine Pancreatic Microsomal Membanes and 35S-methionine. The proteins were spun through a 3% sucrose cushion and then run on a 15% SDS-PAGE gel to determine membrane presence. (3749)

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Nature 436, 290-293. Selective inhibition of cotranslational translocation of vascular cell adhesion molecule 1. 2007

Besemer, J., Harant, H., Wang, S., Oberhauser, B., Marquardt, K., Foster, C.A., Schreiner, E.P., de Vries, J.E., Dascher-Nadel, C. and Lindley, I.J.D.

Notes: Vascular cell adhesion molecule 1 (VCAM1) is associated with several chronic inflammatory conditions. CAM741 is a fungus-derived cyclopeptide that inhibits VCAM1 expression in endothelial cells. This study investigated the mechanism by which this inhibition occurs. HEK293 cells transfected with a VCAM1 expression vector and exposed to CAM741 expressed fully glycosylated VCAM1, indicating that the inhibitor compound did not affect protein production. Production of VCAM1 in the TNT® Coupled Rabbit Reticulocyte Lysate System with and without Canine Microsomal Membranes, and in the presence and absence of CAM741 showed that the appearance of the glycosylated form of the protein was dose-dependently inhibited in the presence of CAM741. This indicated that CAM741 inhibited translocation of VCAM1 across the membranes. The authors further localized the target to the signal peptide region of the VCAM1 protein by examining the effect of various mutations in the signal peptide and other regions of the VCAM1 protein on susceptibility to the inhibitor compound and on translocation. (3580)

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J. Biol. Chem. 282, 29144-29151. The membrane topology of RTN3 and its effect on binding of RTN3 to BACE1 2007

He, W., Shi, Q., Hu, X. and Yan, R.

Notes: The authors of this study determined the membrane topology of reticulon 3 (RTN3), an integral membrane protein that is expressed at high levels in neruons and has been show to negatively regulate the activity of BACE1 (Beta site APP-Cleaving Enzyme). Disruption of RTN3 is associated with incidence of dystrophic neurites in AD brain. RTN3 was translated using the TNT® Quick Coupled Transcription/Translation System in the presence of Canine Microsomal Membranes and labeled using the Transcend™ Non-Radioactive Translation Detection System.

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FEBS Lett. 272, 1704–1717. Novel aggregate formation of a frame-shift mutant protein of tissue-nonspecific alkaline phosphatase is ascribed to three cysteine residues in the C-terminal extension. Retarded secretion and proteasomal degradation. 2005

Komaru, K., Ishida, Y., Amaya, Y., Goseki-Sone, M., Orimo, H. and Oda, K.

Notes: To examine further the phenotype of a known tissue-nonspecific alkaline phosphatase (TNSALP) frameshift mutant, the cDNAs for wildtype TNSALP and TNSALP (1559delT) were subcloned into pALTER®-MAX Vector. Three cysteine residues were replaced with serines using the Altered Sites® II Mammalian Mutagenesis System. The substitution mutations were confirmed by DNA sequencing and the plasmids transfected into CHO cells. The size of the TNSALP (1559delT) product was compared to wildtype TNSALP using the TNT® T7 Coupled Reticulocyte Lysate System and [35S]methionine ⁄ cysteine with or without Canine Pancreatic Microsomal Membranes. The proteins were analyzed using SDS-PAGE and fluorography. (3519)

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J. Biol. Chem. 278(48), 47979-47986. Processing of surfactant protein C requires a type II transmembrane topology directed by juxtamembrane positively charged residues. 2003

Mulugeta, S. and Beers, M.F.

Notes: These authors showed that double-substitution mutation of two N-terminal juxtaposed residues (from positive to neutral charged species) resulted in a reversal of the transmembrane orientation of the protein of interest. For in vitro transcription/translation, they used the TNT® T7 Coupled Reticulocyte Lysate System in the presence of Canine Pancreatic Microsomal Membranes. A protease protection assay and an epitope-specific pull-down assay were used to determine the membrane orientation of the in vitro synthesized protein. (3051)

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J. Clin. Invest. 109, 923-930. The melanin-concentrating hormone receptor 1, a novel target of autoantibody responses in vitiligo 2002

Kemp, E.H., Waterman, E.A., Hawes, B.E., O'Neill, K., Gottumukkala, R.V.S.R.K., Gawkrodger, D.J., Weetman, A.P., and Watson, P.F.

Notes: T4 Polynucleotide Kinase was used to phosphorylate primers before ligating them into a phagemid vector to allow cloning of Sfi I-restricted DNA fragments. Phagemid was prepared from XL1-Blue cells using the Wizard® Minipreps DNA Purification System. Inserts were PCR amplified from the phagemid and purified using the Wizard® PCR Preps DNA Purification System. In separate experiments, the cDNA for the melanin concentrating hormone receptor 1 cDNA was cloned from total melanocyte RNA using MMLV Reverse Transcriptase. In vitro translation of the cDNA was performed using the TnT T7 Coupled Reticulocyte Lysate System and Canine Pancreatic Microsomal Membranes. (2602)

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Proc. Natl. Acad. Sci. USA 98, 1182–1187. From the Cover: Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel 2001

Gonzalez-Perrett, S., Kim, K., Ibarra, C., Damiano, A.E., Zotta, E., Batelli, M., Harris, P.C., Reisin, I.L., Arnaout, M.A. and Cantiello, H.F.

Notes: The SV Total RNA Isolation System was used to isolated RNA from the syncytiotrophoblast of human term placentas. The isolated RNA was used for RT-PCR with M-MLV Reverse Transcriptase used for the RT reaction. The 110 kDa PKD2 protein was expressed in vitro with the TNT® T7 Coupled Reticulocyte Lysate System with and without Canine Pancreatic Microsomal Membranes. The channel activity of the expressed protein was examined and the functional channel could be inhibited by known inhibitors. Expressing the luciferase control with the membranes did not produce the same effect. (2187)

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J. Biol. Chem. 274, 31286-31290.. A novel human apolipoprotein (apoM) 1999

Xu, N., Dahlback, B.

Notes: The cDNA for ApoM was translated with the TNT® Coupled Reticulocyte Lysate System in the presence or absence of the Canine Pancreatic Microsomal Membranes (CMMs). The protein had a higher apparent molecular weight in the presence of the CMMs and the molecular weight was returned to that in the absence of CMMs by treatment with PNGase. (0125)

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J. Biol. Chem. 274, 9029-9037. Mutant vasopressin precursors that cause autosomal dominant neurohypophyseal diabetes isipidus retain dimerization and impair the secretion of wild-type proteins. 1999

Ito, M., Yu, R.N., Jameson, J.L.

Notes: Wildtype arginine vasopressin and wildtype arginine vasopressin with a Myc-His tag were separately translated in vitro with the TNT® Coupled Reticulocyte Lysate System in the presence of Canine Pancreatic Microsomal Membranes (CMMs). The translated proteins were allowed to interact and the complex was brought down via the His tag. (0962)

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J. Biol. Chem. 274, 28762-28770. The N-terminal anchor sequences of 11beta-hydroxysteroid dehydrogenases determine their orientation in the endoplasmic reticulum membrane. 1999

Odermatt, A., Arnold, P., Stauffer, A., Frey, B.M., Frey, F.J.

Notes: Various constructs prepared in pCDNA3 (Invitrogen) were expressed in the TNT® T7 Quick System in the presence of Canine Pancreatic Microsomal Membranes. The orientation of the proteins in the membranes were determined with proteinase K digests with and without Triton® X-100 present. Good detail is provided for the digests. (0587)

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J. Biol. Chem. 274, 457-463. Topology of Euglena chloroplast protein precursors within endoplasmic reticulum to Golgi to chloroplast transport vesicles. 1999

Sulli, C., Fang, Z., Muchhal, U., Schwartzbach, S. D.

Notes: Rabbit Reticulocyte Lysate and Canine Pancreatic Microsomal Membranes (CMMs) were used to study the stop-transfer sequences of pLHCPII. (0316)

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Mol. Cell 1, 565-574. A novel human WD protein, h-betaTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif 1998

Margottin, F., Bour, S.P., Durand, H., Selig, L., Benichou, S., Richard, V., Thomas, D., Strebel, K., Benarous, R.

Notes: The protein Vpu or a mutant Vpu were translated with the Rabbit Reticulocyte Lysate System in the presence of Canine Pancreatic Microsomal Membranes. The h-betaTrCP and a mutant were translated in the absence of the membranes. The h-betaTrCP translation reactions were mixed with the Vpu reactions, incubated then centrifuged. The pellet and supernatants were analyzed for the presence of the h-βTrCP protein. (0731)

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Proc. Natl. Acad. Sci. USA 95, 11336-11341. Attractin (DPPT-L), a member of the CUB family of cell adhesion and guidance proteins, is secreted by activated human T lymphocytes and modulates immune cell interactions. 1998

Duke-Cohan, J.S., Gu, J., McLaughlin, D.F., Xu, Y., Freeman, G.J., Schlossman, S.F.

Notes: The TNT® T7 Quick Coupled Reticulocyte System was used to express the 134kDa Attractin protein. In the presence of Canine Pancreatic Microsomal Membranes (CMMs), the Attractin protein attained its wild-type 175kDa molecular weight. (1204)

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J. Immunol. 160, 2297-2307. Characterization of the interactions between MHC class I subunits: a systematic approach for the engineering of higher affinity variants of beta 2-microglobulin. 1998

Shields, M. J., Assefi, N., Hodgson, W., Kim, E. J., Ribaudo, R.K.

Notes: The authors co-translated mRNAs for beta 2 microglobulin and MHC class I proteins in Flexi® Rabbit Reticulocyte Lysate System with Canine Pancreatic Microsomal Membranes (CMMs). They generated mRNAs using RiboMAX™ T7 Large Scale RNA Production System. Treated transcription reactions with RQ1 RNase-Free DNase I after transcription to remove template DNA. (0393)

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Biochemistry 37, 10134-10143. DNaseY: a rat DNaseI-like gene coding for a constitutively expressed chromatin-bound endonuclease. 1998

Liu, Q.Y., Pandey, S., Singh, R.K., Lin, W., Ribecco, M., Borowy Borowski, H., Smith, B., LeBlanc, J., Walker, P.R., Sikorska, M.

Notes: The authors used the PolyATtract® mRNA Isolation System IV to isolate mRNA from total RNA and the Wizard® PCR Preps DNA Purification Resin to purify a first-strand cDNA synthesis product.  TNT® T7 Coupled in vitro Transcription/Translation Reticulocyte Lysate System was used to synthesize radiolabeled DNaseY. And to test for signal peptide function they added Canine Pancreatic Microsomal Membranes (CMMs). (0779)

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J. Biol. Chem. 273, 23629. Expression cloning and characterization of a transporter for large neutral amino acids activated by the heavy chain of 4F2 antigen (CD98). 1998

Kanai, Y., Segawa, H., Miyamoto, K., Uchino, H., Takeda, E., Endou, H.

Notes: The L-type amino acid transporter 1 (LAT1) cloned in this study from glioma cells was translated in vitro with and without Canine Pancreatic Microsomal Membranes (CMMs) using Rabbit Reticulocyte Lysate (RRL). LAT1 is a 56kDa protein with 12 putative transmembrane domains and could be expressed in RRL with and without CMMs. No change in molecular weight was noted for the protein in either case. Another protein used in this study, the CD98 heavy chain of 65kDa, was translated and glycosylated by RRL and CMMs. The glycosylation was removed with endoH. (0955)

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J. Biol. Chem. 273, 31947-31955. gamma-secretase cleavage is distinct from endoplasmic reticulum degradation of the transmembrane domain of the amyloid precursor protein. 1998

Bunnell, W. L. , Pham, H. V. , Glabe, C. G.

Notes: Th authors used Promega's TNT® Coupled Reticulocyte Lysate System and Canine Pancreatic Microsomal Membranes (CMMs) in initial characterization of an assay for processing of a chimeric APP molecule. (1373)

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Hepatology 27, 254-263. Hepatitis B virus with antigenically alter hepatitis B surface antigen is selected by high-dose hepatitis B immune globulin after liver transplantation 1998

Protzer-Knolle, U., Naumann, U., Bartenschlager, R., Berg, T., Hoff, U., Meyer zum Buschenfeldee, K.-H., Neuhaus, P., Gerken, G.

Notes: Several variant hepatitis B isolates were subjected to PCR to isolate the surface antigen cDNA. The PCR products were cloned and subjected to in vitro transcription/translation with the TNT® Coupled Reticulocyte Lysate System in the presence of Canine Pancreatic Microsomal Membranes (CMMs). The amount of microsomal membranes was adjusted to give the approximate ratios of wild-type glycosylated and unglycosylated forms. The variants were then tested for immunoprecipitation with a commonly used anti-hepatitis B surface antigen pAb. Only one of the variants was immunoprecipitated. (0520)

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J. Biol. Chem. 273, 23080. KCR1, a membrane protein that facilitates functional expression of non-inactivating K+ currents associates with rat EAG voltage-dependent K+ channels. 1998

Hoshi, N., Takahashi, H., Shahidullah, M., Yokoyama, S., Higashida, H.

Notes: The KCR1 protein, with its putative 12 transmembrane domains, were translated with Rabbit Reticulocyte Lysate with and without Canine Pancreatic Microsomal Membranes. The translated proteins were also treated with endoglycosidase H as directed in referenced protocols. (1014)

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J. Biol. Chem. 273, 35008-35015. Molecular cloning and characterization of a novel retinoic acid-inducible gene that encodes a putative G protein-coupled receptor. 1998

Cheng, Y. , Lotan, R.

Notes: These authors used the TNT® T7 Coupled Reticulocyte Lysate System together with Canine Pancreatic Microsomal Membranes (CMMs) to show post-translational modification of RAIG1. They also used RQ1 RNase-free DNase to treat RNA samples prior to cDNA synthesis. (1337)

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J. Biol. Chem. 273, 30973-30978. Protein transport into 'complex' diatom plastids utilizes two different targeting signals. 1998

Lang, M., Apt, K.E., Kroth, P.G.

Notes: The authors used TNT® Coupled Reticulocyte Lysate Systems together with Canine Pancreatic Microsomal Membranes (CMM) to perform heterologous import experiments with trypsin protection of a diatom nuclear-encoded plastid protein. (0836)

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Biophys. J. 75, 2291-2301. Subunit stoichiometry of a core conduction element in a cloned epithelial amiloride-sensitive Na+ channel 1998

Berdiev, B.K, Karlson, K.H., Jovov, B., Ripoll, P.J., Morris, R., Loffing-Cueni, D., Halpin, P., Stanton, B.A., Kleyman, T.R. and Ismailov, I.I.

Notes: The alpha-subunit of the cloned wild-type and mutant epithelial Na+ channel was expressed in vitro using a TNT® Rabbit Reticulocyte Lysate System in the presence of Canine Pancreatic Microsomal Membranes (CMMs). The translation reaction was mixed with various amounts of phosphatidylethanolamine, phosphatidylserine, phosphatidylcholine and Triton X-100 to reconstitute a proteoliposome (more detail on the purification and reconstitution are provided in the paper). The resulting proteoliposomes were used for electrophysiology experiments. (2236)

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J. Biol. Chem. 273, 35362-35370. The 72-kDa component of signal recognition particle is cleaved during apoptosis. 1998

Utz, P. J., Hottelet, M., Le, T. M., Kim, S. J., Geiger, M. E., van Venrooij, W. J., Anderson, P.

Notes: The authors incubated Canine Pancreatic Microsomal Membranes (CMMs) with various caspases to show cleavage of SRP 72. The treated membranes were incubated with β-lactamase made in Rabbit Reticulocyte Lysate and the effect of cleavage of SRP 72 on processing/transport of β-lactamase was evaluated. (0210)

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J. Biol. Chem. 273, 25880-25888. UDP-galactose:ceramide galactosyltransferase is a class I integral membrane protein of the endoplasmic reticulum. 1998

Sprong, H., Kruithof, B., Leijendekker, R., Slot, J. W., van Meer, G., van der Sluijs, P.

Notes: The authors used the TNT® T7 Coupled Reticulocyte Lysate System and Canine Pancreatic Microsomal Membranes (CMMs) to make UDP-galactose:ceramide galactosyltransferase (CGalT) to test antibodies for their ability to immunoprecipitate this protein. (0364)

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Biochemistry 36, 1287-1294. Association of domains within the cystic fibrosis transmembrane conductance regulator. 1997

Ostedgaard, L.S., Rich, D.P., DeBerg, L.G., Welsh, M.J.

Notes: Cystic fibrosis transmembrane conductance regulator (CFTR) was expressed in the TNT® Coupled Reticulocyte Lysate System to confirm its molecular weight. Translation was performed with Canine Pancreatic Microsomal Membranes (CMMs) to verify that the protein is integrated into the membrane. Further, the electrophoretic mobility of CFTR suggests that it is glycosylated. (0570)

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