Structured Review

Promega moloney murine leukemia virus
Moloney Murine Leukemia Virus, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/moloney murine leukemia virus/product/Promega
Average 99 stars, based on 78 article reviews
Price from $9.99 to $1999.99
moloney murine leukemia virus - by Bioz Stars, 2020-09
99/100 stars

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Reverse Transcription Polymerase Chain Reaction:

Article Title: OsTIR1 and OsAFB2 Downregulation via OsmiR393 Overexpression Leads to More Tillers, Early Flowering and Less Tolerance to Salt and Drought in Rice
Article Snippet: .. The total RNA reverse transcription reaction was performed with a two-step RT-PCR kit (Promega, Cat.# M 1701) on 2 µg of total RNA according to the product manual. .. Expression detection by real-time quantitative PCR Gene expression was analyzed by quantitative real time RT-PCR and semi-quantitative RT-PCR using the primers listed in .

Polymerase Chain Reaction:

Article Title: Calcium-dependent regulation of the cell cycle via a novel MAPK-NF-?B pathway in Swiss 3T3 cells
Article Snippet: .. 2 μg of RNA was used to perform reverse transcriptase PCR (using 200 U M-MLV reverse transcriptase; Promega). .. For PCR amplification, 5 μl of RT products were incubated with 20 pmol of specific primers and 1 U of Taq DNA polymerase (Promega).

Incubation:

Article Title: A cypovirus VP5 displays the RNA chaperone-like activity that destabilizes RNA helices and accelerates strand annealing
Article Snippet: .. After incubation, 4 μl of the RT buffer, 1 μl of 0.1 M DTT, 5 U RNasin and 0.5 μl M-MLV reverse transcriptase (Promega) were supplemented and reacted at 25°C for 30 min. ..

other:

Article Title: Relaxed Primer Specificity Associated with Reverse Transcriptases Encoded by the pFOXC Retroplasmids of Fusarium oxysporum
Article Snippet: In a direct comparison with AMV RT and MMLV RT, the pFOXC RT was significantly more proficient at extending a DNA primer that had only 10 nt of complementarity to the 3′ termini of the RNA templates.

Article Title: Relaxed Primer Specificity Associated with Reverse Transcriptases Encoded by the pFOXC Retroplasmids of Fusarium oxysporum
Article Snippet: The ability to extend snapped-back RNAs is a common characteristic of retroviral RTs, and analogous RNA-cDNA hybrid products were also formed in reactions containing MMLV RT.

Article Title: Relaxed Primer Specificity Associated with Reverse Transcriptases Encoded by the pFOXC Retroplasmids of Fusarium oxysporum
Article Snippet: Interestingly, the major cDNA products obtained with MMLV RT were significantly shorter (73, 76, and 82 nt) than those obtained with the MN-treated pFOXC RT.

Article Title: Relaxed Primer Specificity Associated with Reverse Transcriptases Encoded by the pFOXC Retroplasmids of Fusarium oxysporum
Article Snippet: Significantly, these products were absent from reactions with MMLV RT (Fig. , lanes 9 and 10) and were found in reactions lacking RNA templates (see below).

RT Lamp Assay:

Article Title: Rapid detection of wheat yellow mosaic virus by reverse transcription loop-mediated isothermal amplification
Article Snippet: .. For each primer set, AMV and M-MLV RT-LAMP was performed and similar results were obtained, therefore, M-MLV reverse transcriptase was chosen for the subsequent RT-LAMP assay because of its relatively cheap price (Figure ). ..

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  • 80
    Promega momulv gag pol
    Schematic representation of chimeric envelopes, and results of infection with vectors bearing various SSAV, GALV-S, and SSAV/GALV-S chimeric envelopes in E36 and MDTFPit1 cells. For each construct, sequences from the SSAV envelope are in white, and those from GALV-S envelope are in black. A, VRA; B, VRB. Plasmids with various envelope chimeras were cotransfected with plasmids encoding <t>MoMuLV</t> core proteins and packageable genome into 293T cells. The supernatant was harvested and used to infect E36 and MDTFPit1 cells as described in Materials and Methods. The titers were averaged from at least three independent experiments and are expressed as mean number of <t>β-galactosidase-expressing</t> cells ± standard deviation of the mean.
    Momulv Gag Pol, supplied by Promega, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/momulv gag pol/product/Promega
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    momulv gag pol - by Bioz Stars, 2020-09
    80/100 stars
      Buy from Supplier

    94
    Promega moloney murine leukemia virus reverse transcriptase
    Higher proliferation rate of MEFs correlates with lower reprogramming efficiency. A and B, time course study of the proliferation rate of MEFs and the reprogramming efficiency with OSK and serially diluted c- Myc viruses. MEFs were transduced with OSK plus c-Myc in 5-fold serial dilutions (including zero concentration). The number of total cells ( A ) and the percentage of GFP + cells ( B ) were monitored every other day during the reprogramming process. C, proliferation rates of two OSK-iPS and two OSKM-iPS clones. Cell numbers were normalized to the value obtained on day 1. D, quantitative PCR analysis of the expression levels of Cdk 1 / 2 / 4 in OSK or OSKM iPS clones. The expression level of each gene was normalized to that of β -actin in the same sample and then normalized to MEFs. E, characterization of cell death in OSK- or OSKM-mediated reprogramming using propidium iodide staining and FACS analysis. F and G , MEFs were infected with OSKM or OSK in combination with a <t>Moloney</t> murine leukemia virus 5′ LTR promoter-driven dsRed virus and seeded at different densities in a 96-well plate, the number of GFP + dsRed − colonies were counted at day 14 ( G ), the number of dsRed + cells were recorded at day 6, and the reprogramming efficiency ( H ) was calculated (number of GFP + dsRed − colonies/number of dsRed + cells). *, p
    Moloney Murine Leukemia Virus Reverse Transcriptase, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 939 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/moloney murine leukemia virus reverse transcriptase/product/Promega
    Average 94 stars, based on 939 article reviews
    Price from $9.99 to $1999.99
    moloney murine leukemia virus reverse transcriptase - by Bioz Stars, 2020-09
    94/100 stars
      Buy from Supplier

    90
    Promega momlv
    Interaction of <t>MoMLV</t> RT with eRF1. ( a ) Interface between the <t>RNase</t> H domain of MoMLV RT and eRF1-C. Residues involved in the interaction are shown as sticks and labelled. ( b ) GST pull-down assay. GST tagged WT MoMLV RNase H and its mutants on beads were used to bind His-tagged eRF1-C and its variants.
    Momlv, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/momlv/product/Promega
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    momlv - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

    Image Search Results


    Schematic representation of chimeric envelopes, and results of infection with vectors bearing various SSAV, GALV-S, and SSAV/GALV-S chimeric envelopes in E36 and MDTFPit1 cells. For each construct, sequences from the SSAV envelope are in white, and those from GALV-S envelope are in black. A, VRA; B, VRB. Plasmids with various envelope chimeras were cotransfected with plasmids encoding MoMuLV core proteins and packageable genome into 293T cells. The supernatant was harvested and used to infect E36 and MDTFPit1 cells as described in Materials and Methods. The titers were averaged from at least three independent experiments and are expressed as mean number of β-galactosidase-expressing cells ± standard deviation of the mean.

    Journal: Journal of Virology

    Article Title: Simian Sarcoma-Associated Virus Fails To Infect Chinese Hamster Cells despite the Presence of Functional Gibbon Ape Leukemia Virus Receptors

    doi:

    Figure Lengend Snippet: Schematic representation of chimeric envelopes, and results of infection with vectors bearing various SSAV, GALV-S, and SSAV/GALV-S chimeric envelopes in E36 and MDTFPit1 cells. For each construct, sequences from the SSAV envelope are in white, and those from GALV-S envelope are in black. A, VRA; B, VRB. Plasmids with various envelope chimeras were cotransfected with plasmids encoding MoMuLV core proteins and packageable genome into 293T cells. The supernatant was harvested and used to infect E36 and MDTFPit1 cells as described in Materials and Methods. The titers were averaged from at least three independent experiments and are expressed as mean number of β-galactosidase-expressing cells ± standard deviation of the mean.

    Article Snippet: The following three plasmids were transfected into 293T cells by the calcium phosphate precipitation method (Promega): (i) 10 μg of pRT43.2TnIsbgal , a Moloney MuLV (MoMuLV)-based packageable genome containing the packaging signal and the β-galactosidase gene coding sequence; (ii) 2.5 μg of MoMuLV gag-pol -expressing plasmid ( ); and (iii) 5 μg of pCI-neo (Promega) plasmid with GALV-S or SSAV envelope coding region.

    Techniques: Infection, Construct, Expressing, Standard Deviation

    Higher proliferation rate of MEFs correlates with lower reprogramming efficiency. A and B, time course study of the proliferation rate of MEFs and the reprogramming efficiency with OSK and serially diluted c- Myc viruses. MEFs were transduced with OSK plus c-Myc in 5-fold serial dilutions (including zero concentration). The number of total cells ( A ) and the percentage of GFP + cells ( B ) were monitored every other day during the reprogramming process. C, proliferation rates of two OSK-iPS and two OSKM-iPS clones. Cell numbers were normalized to the value obtained on day 1. D, quantitative PCR analysis of the expression levels of Cdk 1 / 2 / 4 in OSK or OSKM iPS clones. The expression level of each gene was normalized to that of β -actin in the same sample and then normalized to MEFs. E, characterization of cell death in OSK- or OSKM-mediated reprogramming using propidium iodide staining and FACS analysis. F and G , MEFs were infected with OSKM or OSK in combination with a Moloney murine leukemia virus 5′ LTR promoter-driven dsRed virus and seeded at different densities in a 96-well plate, the number of GFP + dsRed − colonies were counted at day 14 ( G ), the number of dsRed + cells were recorded at day 6, and the reprogramming efficiency ( H ) was calculated (number of GFP + dsRed − colonies/number of dsRed + cells). *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Proliferation Rate of Somatic Cells Affects Reprogramming Efficiency *

    doi: 10.1074/jbc.M112.403881

    Figure Lengend Snippet: Higher proliferation rate of MEFs correlates with lower reprogramming efficiency. A and B, time course study of the proliferation rate of MEFs and the reprogramming efficiency with OSK and serially diluted c- Myc viruses. MEFs were transduced with OSK plus c-Myc in 5-fold serial dilutions (including zero concentration). The number of total cells ( A ) and the percentage of GFP + cells ( B ) were monitored every other day during the reprogramming process. C, proliferation rates of two OSK-iPS and two OSKM-iPS clones. Cell numbers were normalized to the value obtained on day 1. D, quantitative PCR analysis of the expression levels of Cdk 1 / 2 / 4 in OSK or OSKM iPS clones. The expression level of each gene was normalized to that of β -actin in the same sample and then normalized to MEFs. E, characterization of cell death in OSK- or OSKM-mediated reprogramming using propidium iodide staining and FACS analysis. F and G , MEFs were infected with OSKM or OSK in combination with a Moloney murine leukemia virus 5′ LTR promoter-driven dsRed virus and seeded at different densities in a 96-well plate, the number of GFP + dsRed − colonies were counted at day 14 ( G ), the number of dsRed + cells were recorded at day 6, and the reprogramming efficiency ( H ) was calculated (number of GFP + dsRed − colonies/number of dsRed + cells). *, p

    Article Snippet: About 1.5 μg of RNA was used to synthesize cDNA using Random Hexamer Primer and Moloney murine leukemia virus reverse transcriptase (Promega) according to the manufacturer's protocol.

    Techniques: Transduction, Concentration Assay, Clone Assay, Real-time Polymerase Chain Reaction, Expressing, Staining, FACS, Infection

    Expression of intestinal SST receptors (SSTRs) in mice and Caco-2 cells. Total RNA was isolated from mouse intestinal mucosa and Caco-2 cells. Reverse transcription reaction was performed with Moloney murine leukemia virus reverse transcriptase and random primers. RT-PCR was used to amplify SSTR cDNAs with SSRT gene-specific primers. PCR products were separated on 1.5% agarose gel and visualized after ethidium bromide staining. A : PCR amplification of SSTRs from mouse intestine. B : PCR amplification of SSTRs from Caco-2 cells.

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Somatostatin stimulates intestinal NHE8 expression via p38 MAPK pathway

    doi: 10.1152/ajpcell.00421.2010

    Figure Lengend Snippet: Expression of intestinal SST receptors (SSTRs) in mice and Caco-2 cells. Total RNA was isolated from mouse intestinal mucosa and Caco-2 cells. Reverse transcription reaction was performed with Moloney murine leukemia virus reverse transcriptase and random primers. RT-PCR was used to amplify SSTR cDNAs with SSRT gene-specific primers. PCR products were separated on 1.5% agarose gel and visualized after ethidium bromide staining. A : PCR amplification of SSTRs from mouse intestine. B : PCR amplification of SSTRs from Caco-2 cells.

    Article Snippet: Total RNA (500 ng) was reverse transcribed to cDNA by Moloney murine leukemia virus reverse transcriptase (Promega).

    Techniques: Expressing, Mouse Assay, Isolation, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Agarose Gel Electrophoresis, Staining, Amplification

    Interaction of MoMLV RT with eRF1. ( a ) Interface between the RNase H domain of MoMLV RT and eRF1-C. Residues involved in the interaction are shown as sticks and labelled. ( b ) GST pull-down assay. GST tagged WT MoMLV RNase H and its mutants on beads were used to bind His-tagged eRF1-C and its variants.

    Journal: Nature Communications

    Article Title: Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus

    doi: 10.1038/ncomms12070

    Figure Lengend Snippet: Interaction of MoMLV RT with eRF1. ( a ) Interface between the RNase H domain of MoMLV RT and eRF1-C. Residues involved in the interaction are shown as sticks and labelled. ( b ) GST pull-down assay. GST tagged WT MoMLV RNase H and its mutants on beads were used to bind His-tagged eRF1-C and its variants.

    Article Snippet: Codon-optimized RNase H domains from HIV-1 or MoMLV containing the catalytic D524N mutation or Nano luciferase (Promega) were cloned in-frame downstream of MLVPK or mCherry as indicated.

    Techniques: Pull Down Assay

    MoMLV RNase H enhances stop codon read-through and stabilizes mRNAs. ( a ) Schematic of tet-regulated reporter mRNAs used in read-through and mRNA decay assays. The indicated RNase H variants were inserted downstream of the MLVPK, in-frame with the GFP and mCherry ORFs. The red dot represents the stop codon. ( b ) Translational read-through assays using dual-fluorescent-protein reporters containing the indicated MLVPK and RNase H variants. The ratio of mCherry:GFP from each experimental construct was normalized to that arising from a sequence-matched control lacking a stop codon between GFP and mCherry. Error bars indicate s.d. ( n =7; **** P

    Journal: Nature Communications

    Article Title: Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus

    doi: 10.1038/ncomms12070

    Figure Lengend Snippet: MoMLV RNase H enhances stop codon read-through and stabilizes mRNAs. ( a ) Schematic of tet-regulated reporter mRNAs used in read-through and mRNA decay assays. The indicated RNase H variants were inserted downstream of the MLVPK, in-frame with the GFP and mCherry ORFs. The red dot represents the stop codon. ( b ) Translational read-through assays using dual-fluorescent-protein reporters containing the indicated MLVPK and RNase H variants. The ratio of mCherry:GFP from each experimental construct was normalized to that arising from a sequence-matched control lacking a stop codon between GFP and mCherry. Error bars indicate s.d. ( n =7; **** P

    Article Snippet: Codon-optimized RNase H domains from HIV-1 or MoMLV containing the catalytic D524N mutation or Nano luciferase (Promega) were cloned in-frame downstream of MLVPK or mCherry as indicated.

    Techniques: Construct, Sequencing

    The RNase H domain of MoMLV RT outcompetes eRF3 for binding to eRF1. ( a ) Superposition of the RNase H/eRF1-C complex with the eRF1/eRF3 complex (PDB accession code: 3E1Y) at eRF1-C domain. The overlapping interface suggests that MoMLV RT and eRF3 are mutually exclusive for binding to eRF1. eRF3 domain 3 is shown in cartoon (blue) covered with grey transparent surface. eRF3 domain 2 and eRF1-C domain in eRF1/eRF3 complex are not displayed for clarity. ( b , c ) Representative ITC titrations of WT RNase H and mutant A589K to the eRF1/eRF3 complex. The upper panels show the binding isotherms and the lower panels show the integrated heat for each injection fitted to a single-site model.

    Journal: Nature Communications

    Article Title: Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus

    doi: 10.1038/ncomms12070

    Figure Lengend Snippet: The RNase H domain of MoMLV RT outcompetes eRF3 for binding to eRF1. ( a ) Superposition of the RNase H/eRF1-C complex with the eRF1/eRF3 complex (PDB accession code: 3E1Y) at eRF1-C domain. The overlapping interface suggests that MoMLV RT and eRF3 are mutually exclusive for binding to eRF1. eRF3 domain 3 is shown in cartoon (blue) covered with grey transparent surface. eRF3 domain 2 and eRF1-C domain in eRF1/eRF3 complex are not displayed for clarity. ( b , c ) Representative ITC titrations of WT RNase H and mutant A589K to the eRF1/eRF3 complex. The upper panels show the binding isotherms and the lower panels show the integrated heat for each injection fitted to a single-site model.

    Article Snippet: Codon-optimized RNase H domains from HIV-1 or MoMLV containing the catalytic D524N mutation or Nano luciferase (Promega) were cloned in-frame downstream of MLVPK or mCherry as indicated.

    Techniques: Binding Assay, Mutagenesis, Injection

    Structural explanation of why HIV RT cannot interact with eRF1. ( a ) Cartoon representation of the RNase H domain of MoMLV RT. ( b ) The RNase H domain of HIV RT, which is coloured in cyan with its helix α2 highlighted in purple. ( c ) Sequence alignment of the helix α2 from various genera of retroviruses. MoMLV, XMRV and PERV (Porcine endogenous retrovirus) belong to gammaretrovirus. HIV-1 and EIVA (Equine infectious anaemia) are lentivirus. BLV (Bovine leukemia virus), HFV (Human foamy virus), MPMV (Mason pfizer monkey virus) and RSV (Rous sarcoma virus) belong to deltaretrovirus, spumaretrovirus, betaretrovirus and alpharetrovirus respectively. ( d ) Superposition of MoMLV RT and HIV RT p66 (PDB accession code: 1HYS) at their polymerase domains. HIV RT p66 except RNase H domain and p51 subunits are shown as surfaces coloured in cyan and salmon, respectively.

    Journal: Nature Communications

    Article Title: Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus

    doi: 10.1038/ncomms12070

    Figure Lengend Snippet: Structural explanation of why HIV RT cannot interact with eRF1. ( a ) Cartoon representation of the RNase H domain of MoMLV RT. ( b ) The RNase H domain of HIV RT, which is coloured in cyan with its helix α2 highlighted in purple. ( c ) Sequence alignment of the helix α2 from various genera of retroviruses. MoMLV, XMRV and PERV (Porcine endogenous retrovirus) belong to gammaretrovirus. HIV-1 and EIVA (Equine infectious anaemia) are lentivirus. BLV (Bovine leukemia virus), HFV (Human foamy virus), MPMV (Mason pfizer monkey virus) and RSV (Rous sarcoma virus) belong to deltaretrovirus, spumaretrovirus, betaretrovirus and alpharetrovirus respectively. ( d ) Superposition of MoMLV RT and HIV RT p66 (PDB accession code: 1HYS) at their polymerase domains. HIV RT p66 except RNase H domain and p51 subunits are shown as surfaces coloured in cyan and salmon, respectively.

    Article Snippet: Codon-optimized RNase H domains from HIV-1 or MoMLV containing the catalytic D524N mutation or Nano luciferase (Promega) were cloned in-frame downstream of MLVPK or mCherry as indicated.

    Techniques: Sequencing

    Structure of the MoMLV RT/eRF1 complex. ( a ) Schematic representation of the domain organization of eRF1 and MoMLV RT. Domains N, M, and C of eRF1 are coloured in pink, lightblue and green, respectively. MoMLV RT polymerase domain is coloured in grey and RNase H domain in yellow. ( b ) A ribbon diagram of the MoMLV RT/eRF1 complex. The colouring scheme is as in a . The helix α2 of RNase H domain is highlighted in red. ( c ) The RNase H/eRF1-C complex structure. The secondary structure elements of RNase H domain are labelled.

    Journal: Nature Communications

    Article Title: Structural basis of suppression of host translation termination by Moloney Murine Leukemia Virus

    doi: 10.1038/ncomms12070

    Figure Lengend Snippet: Structure of the MoMLV RT/eRF1 complex. ( a ) Schematic representation of the domain organization of eRF1 and MoMLV RT. Domains N, M, and C of eRF1 are coloured in pink, lightblue and green, respectively. MoMLV RT polymerase domain is coloured in grey and RNase H domain in yellow. ( b ) A ribbon diagram of the MoMLV RT/eRF1 complex. The colouring scheme is as in a . The helix α2 of RNase H domain is highlighted in red. ( c ) The RNase H/eRF1-C complex structure. The secondary structure elements of RNase H domain are labelled.

    Article Snippet: Codon-optimized RNase H domains from HIV-1 or MoMLV containing the catalytic D524N mutation or Nano luciferase (Promega) were cloned in-frame downstream of MLVPK or mCherry as indicated.

    Techniques: