In Vitro Transcription Translation Reaction, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/in vitro transcription translation reaction/product/Promega
Average 99 stars, based on 39 article reviews
Price from $9.99 to $1999.99
1) Product Images from "Thermoregulation of Meningococcal fHbp, an Important Virulence Factor and Vaccine Antigen, Is Mediated by Anti-ribosomal Binding Site Sequences in the Open Reading Frame"
Article Title: Thermoregulation of Meningococcal fHbp, an Important Virulence Factor and Vaccine Antigen, Is Mediated by Anti-ribosomal Binding Site Sequences in the Open Reading Frame
Journal: PLoS Pathogens
Figure Legend Snippet: Gradual thermoregulation of fHbp-GFP. (A) In vitro transcription/translation assays using DNA from p fHbp- 1C -gfp p fHbp- 5C -gfp or p fHbp- 9C -gfp (number of codons shown above each lane) performed at the indicated temperatures for 1 hr. Samples were subject to Western analysis. (B) Gradual thermoregulation of fHbp-GFP. RNA was isolated from E . coli containing p fHbp- 9C -gfp construct was subjected to in vitro translation at indicated temperatures. Western analysis was performed using antibodies recognising GFP or RecA.
Techniques Used: In Vitro, Western Blot, Isolation, Construct
2) Product Images from "Roles of Asp179 and Glu270 in ADP-Ribosylation of Actin by Clostridium perfringens Iota Toxin"
Article Title: Roles of Asp179 and Glu270 in ADP-Ribosylation of Actin by Clostridium perfringens Iota Toxin
Journal: PLoS ONE
Figure Legend Snippet: In vitro ADP-ribosylation of human β-actin variants. Actin variants were produced in in vitro transcription/translation reaction, using as a matrix plasmids coding for human β-actin gene with the corresponding amino acid substitutions (wild type (WT), R177K, D179A, E270D and E270Q). Afterwards, 1 μl of the in vitro transcription/translation mix was ADP-ribosylated with Ia (150 ng/10 μl in Panel A; 15 and 50 ng/10 μl in Panel B; and 15, 50 or 150 ng/10 μl in Panel C) or left untreated, without toxin (w/o). Reaction mixes were subjected to non-denaturing polyacrylamide gel electrophoresis and autoradiography (shown) to detect 35 S-methionine-labelled actin variants. Arrows on the left indicate position of shifted ADP-ribosylated actin.
Techniques Used: In Vitro, Produced, IA, Polyacrylamide Gel Electrophoresis, Autoradiography
3) Product Images from "Negative regulation of FAK signaling by SOCS proteins"
Article Title: Negative regulation of FAK signaling by SOCS proteins
Journal: The EMBO Journal
Figure Legend Snippet: Fig. 7. SOCS-proteins promote polyubiquitination of FAK. ( A ) COS-7 cells were transiently transfected with HA-FAK (0.5 µg) alone or with wild-type forms of Myc-SOCS-1 or SOCS-3 or their SOCS box-deletion mutants (SOCSΔSB) (1.0 µg). Twenty-four hours after transfection the cells were serum-starved overnight and pretreated with or without β-lactacystin (25 µM) for 4 h prior to pervanadate treatment (50 µM) for 1 h. FAK was immunoprecipitated with an anti-HA antibody, followed by a dissociation and reprecipitation with the same antibody. FAK immunoprecipitates were analyzed by immunoblotting with antibodies against ubiquitin and HA. Total cell lysates were subjected to immunoblotting with anti-Myc antibody to confirm SOCS-protein expression levels. ( B ) In vitro ubiquitination reactions on immunoprecipitated wild-type FAK or FAK-Y397F mutant were performed as described in the Materials and methods in the presence or absence of cell lysates containing the indicated SOCS proteins. The reaction products were separated on SDS–PAGE, transferred onto PVDF membrane, and the blots were probed with anti-ubiquitin antibody (upper panel). Equal loading of the various SOCS proteins was verified by anti-Myc immunoblotting of total cell lysates (lower panel). ( C ) HA-tagged wild-type FAK was generated by a coupled in vitro transcription/translation system. An in vitro ubiquitination assay was performed on the Sepharose-purified FAK as in (B). ( D ) NIH 3T3 cells were transfected with 0.5 µg of plasmid coding for ubiquitin with or without 1.0 µg of SOCS-3ΔSB. Twenty-four hours after transfection, the cells were serum-starved overnight, detached, stimulated or not with PDGF, and either kept in suspension or replaced on FN for 1 or 4 h in the presence of 50 µM pervanadate and 25 µM proteasome inhibitor MG132. Cell lysates were subjected to immunoprecipitation with anti-FAK antibody followed by immunoblotting with antibodies against ubiquitin, FAK, pTyr, SOCS-3 and Myc (upper panels). An isotype-matched IgG was used as a control to demonstrate that anti-FAK antibodies do not unspecifically precipitate SOCS-3 (middle panel). Total cell lysates were subjected to immunoblot with anti-SOCS-3, anti-Myc and anti-tubulin antibodies (bottom three panels).
Techniques Used: Transfection, Immunoprecipitation, Expressing, In Vitro, Mutagenesis, SDS Page, Generated, Ubiquitin Assay, Purification, Plasmid Preparation
4) Product Images from "Imprinting regulation of the murine Meg1/Grb10 and human GRB10 genes; roles of brain-specific promoters and mouse-specific CTCF-binding sites"
Article Title: Imprinting regulation of the murine Meg1/Grb10 and human GRB10 genes; roles of brain-specific promoters and mouse-specific CTCF-binding sites
Journal: Nucleic Acids Research
Figure Legend Snippet: CTCF binds specifically to the Meg1 repeat. ( A ) Specific competition for CTCF binding to the Meg1 repeat was seen for the canonical CTCF- binding sequence of the chicken β- globin FII (as shown in F), but not for the transcription factor recognition sequences of SP1 and AP1 (as shown in S and A) and vice versa. Mouse recombinant CTCF containing a full-length coding sequence was used. There were no DNA-binding factors included in the in vitro reticulocyte transcription/translation reaction mixture without CTCF-containing vector (left most lane). ( B ) The methylated Meg1 repeat was a less effective competitor than the non-methylated sequence.
Techniques Used: Binding Assay, Sequencing, Recombinant, In Vitro, Plasmid Preparation, Methylation
5) Product Images from "Rescue of Very Virulent and Mosaic Infectious Bursal Disease Virus from Cloned cDNA: VP2 Is Not the Sole Determinant of the Very Virulent Phenotype"
Article Title: Rescue of Very Virulent and Mosaic Infectious Bursal Disease Virus from Cloned cDNA: VP2 Is Not the Sole Determinant of the Very Virulent Phenotype
Journal: Journal of Virology
Figure Legend Snippet: Autoradiogram of an SDS-PAGE analysis of a coupled in vitro transcription/translation reaction. (A) Full-length A-segment plasmids of attenuated classical IBDV isolate CEF94 (pHB-36W, lane 1) and wild-type vvIBDV isolate D6948 (pHB-60, lane 2). (B) Full-length B-segment plasmids of CEF94 (pHB-34Z, lane 1) and D6948 (pHB-55, lane 2). (C) Full-length A-segment plasmid of CEF94 (pHB-36W, lane 1) and full-length A-segment plasmid of the classical attenuated IBDV isolate in which either pVP2 (pHB36-vvVP2; lane 2), VP3 (pHB36-vvVP3; lane 3), or VP4 (pHB36-vvVP4; lane 4) has been exchanged. The positions of the viral proteins are on the right. The sizes of the marker proteins (Rainbow marker; Amersham) are on the left.
Techniques Used: SDS Page, In Vitro, Plasmid Preparation, Marker
6) Product Images from "Identification of a structural constituent and one possible site of postembryonic formation of a teleost otolithic membrane"
Article Title: Identification of a structural constituent and one possible site of postembryonic formation of a teleost otolithic membrane
Journal: Proceedings of the National Academy of Sciences of the United States of America
Figure Legend Snippet: In vitro transcription/translation analysis of the SC cDNA. One microgram of a plasmid containing the full-length SC cDNA or the full-length luciferase cDNA as a control were used as substrate for the rabbit reticulocyte-derived coupled in vitro transcription/translation reaction in the presence of [ 35 S]methionine (Amersham). Control reactions in which cDNA template or RNA polymerase was omitted were also prepared and all the reaction products were resolved in 7% polyacrylamide denaturing gels as described. Lanes: NTP, no collagen template, with polymerase; LP, luciferase cDNA plus polymerase (62 kDa); CP, SC cDNA plus polymerase; NP, with collagen template but without polymerase. The arrowhead points to the in vitro transcription/translation product synthesized from the SC cDNA in lane CP.
Techniques Used: In Vitro, Plasmid Preparation, Luciferase, Derivative Assay, Synthesized