hiv 1 rt enzyme  (Worthington Biochemical)


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    Structured Review

    Worthington Biochemical hiv 1 rt enzyme
    Sequence alignment of amino acids 101 to 240 in the RTs of <t>HIV-1</t> HXB2 , RT-SHIV mne , SIV mne , and SIV-RT-YY. Dots indicate residues conserved between the different isolates. Boxed residues indicate residues 181 and 188, which are the residues that were changed to tyrosines in SIV-RT-YY.
    Hiv 1 Rt Enzyme, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hiv 1 rt enzyme/product/Worthington Biochemical
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hiv 1 rt enzyme - by Bioz Stars, 2022-07
    86/100 stars

    Images

    1) Product Images from "In Vitro Characterization of a Simian Immunodeficiency Virus-Human Immunodeficiency Virus (HIV) Chimera Expressing HIV Type 1 Reverse Transcriptase To Study Antiviral Resistance in Pigtail Macaques"

    Article Title: In Vitro Characterization of a Simian Immunodeficiency Virus-Human Immunodeficiency Virus (HIV) Chimera Expressing HIV Type 1 Reverse Transcriptase To Study Antiviral Resistance in Pigtail Macaques

    Journal: Journal of Virology

    doi: 10.1128/JVI.78.24.13553-13561.2004

    Sequence alignment of amino acids 101 to 240 in the RTs of HIV-1 HXB2 , RT-SHIV mne , SIV mne , and SIV-RT-YY. Dots indicate residues conserved between the different isolates. Boxed residues indicate residues 181 and 188, which are the residues that were changed to tyrosines in SIV-RT-YY.
    Figure Legend Snippet: Sequence alignment of amino acids 101 to 240 in the RTs of HIV-1 HXB2 , RT-SHIV mne , SIV mne , and SIV-RT-YY. Dots indicate residues conserved between the different isolates. Boxed residues indicate residues 181 and 188, which are the residues that were changed to tyrosines in SIV-RT-YY.

    Techniques Used: Sequencing

    In vitro RT inhibition with NNRTIs. Representative data are shown in which JC53 BL13+ cells were infected with HIV-1 NFNSX , SIV mne , RT-SHIV mne , or SIV-RT-YY in the presence or absence of multiple concentrations of EFV (A), NVP (B), or UC781 (C). Infections were performed in duplicate, and luciferase measurements were performed in triplicate. Results are expressed as the percent cells infected for each virus with each dilution of drug compared to infection without drug.
    Figure Legend Snippet: In vitro RT inhibition with NNRTIs. Representative data are shown in which JC53 BL13+ cells were infected with HIV-1 NFNSX , SIV mne , RT-SHIV mne , or SIV-RT-YY in the presence or absence of multiple concentrations of EFV (A), NVP (B), or UC781 (C). Infections were performed in duplicate, and luciferase measurements were performed in triplicate. Results are expressed as the percent cells infected for each virus with each dilution of drug compared to infection without drug.

    Techniques Used: In Vitro, Inhibition, Infection, Luciferase

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  • 86
    Worthington Biochemical hiv 1 rt enzyme
    Sequence alignment of amino acids 101 to 240 in the RTs of <t>HIV-1</t> HXB2 , RT-SHIV mne , SIV mne , and SIV-RT-YY. Dots indicate residues conserved between the different isolates. Boxed residues indicate residues 181 and 188, which are the residues that were changed to tyrosines in SIV-RT-YY.
    Hiv 1 Rt Enzyme, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hiv 1 rt enzyme/product/Worthington Biochemical
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hiv 1 rt enzyme - by Bioz Stars, 2022-07
    86/100 stars
      Buy from Supplier

    93
    Worthington Biochemical reagents recombinant hiv 1 reverse transcriptase
    Alignment of sequences flanking RNA 5′ end-directed cleavage sites recognized by <t>HIV-1</t> RNase H ). In the center column, the sequence surrounding each cleavage site is given, with the location of the cleavage site represented as a gap. The right column gives the position of each cleavage site counting from the 5′ end of the RNA.
    Reagents Recombinant Hiv 1 Reverse Transcriptase, supplied by Worthington Biochemical, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/reagents recombinant hiv 1 reverse transcriptase/product/Worthington Biochemical
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    reagents recombinant hiv 1 reverse transcriptase - by Bioz Stars, 2022-07
    93/100 stars
      Buy from Supplier

    Image Search Results


    Sequence alignment of amino acids 101 to 240 in the RTs of HIV-1 HXB2 , RT-SHIV mne , SIV mne , and SIV-RT-YY. Dots indicate residues conserved between the different isolates. Boxed residues indicate residues 181 and 188, which are the residues that were changed to tyrosines in SIV-RT-YY.

    Journal: Journal of Virology

    Article Title: In Vitro Characterization of a Simian Immunodeficiency Virus-Human Immunodeficiency Virus (HIV) Chimera Expressing HIV Type 1 Reverse Transcriptase To Study Antiviral Resistance in Pigtail Macaques

    doi: 10.1128/JVI.78.24.13553-13561.2004

    Figure Lengend Snippet: Sequence alignment of amino acids 101 to 240 in the RTs of HIV-1 HXB2 , RT-SHIV mne , SIV mne , and SIV-RT-YY. Dots indicate residues conserved between the different isolates. Boxed residues indicate residues 181 and 188, which are the residues that were changed to tyrosines in SIV-RT-YY.

    Article Snippet: A standard curve was created using HIV-1 RT enzyme (Worthington, Lakewood, N.J.) diluted between 10−2 and 10−10 U/μl in the same buffer used for the samples and assayed in triplicate.

    Techniques: Sequencing

    In vitro RT inhibition with NNRTIs. Representative data are shown in which JC53 BL13+ cells were infected with HIV-1 NFNSX , SIV mne , RT-SHIV mne , or SIV-RT-YY in the presence or absence of multiple concentrations of EFV (A), NVP (B), or UC781 (C). Infections were performed in duplicate, and luciferase measurements were performed in triplicate. Results are expressed as the percent cells infected for each virus with each dilution of drug compared to infection without drug.

    Journal: Journal of Virology

    Article Title: In Vitro Characterization of a Simian Immunodeficiency Virus-Human Immunodeficiency Virus (HIV) Chimera Expressing HIV Type 1 Reverse Transcriptase To Study Antiviral Resistance in Pigtail Macaques

    doi: 10.1128/JVI.78.24.13553-13561.2004

    Figure Lengend Snippet: In vitro RT inhibition with NNRTIs. Representative data are shown in which JC53 BL13+ cells were infected with HIV-1 NFNSX , SIV mne , RT-SHIV mne , or SIV-RT-YY in the presence or absence of multiple concentrations of EFV (A), NVP (B), or UC781 (C). Infections were performed in duplicate, and luciferase measurements were performed in triplicate. Results are expressed as the percent cells infected for each virus with each dilution of drug compared to infection without drug.

    Article Snippet: A standard curve was created using HIV-1 RT enzyme (Worthington, Lakewood, N.J.) diluted between 10−2 and 10−10 U/μl in the same buffer used for the samples and assayed in triplicate.

    Techniques: In Vitro, Inhibition, Infection, Luciferase

    Alignment of sequences flanking RNA 5′ end-directed cleavage sites recognized by HIV-1 RNase H ). In the center column, the sequence surrounding each cleavage site is given, with the location of the cleavage site represented as a gap. The right column gives the position of each cleavage site counting from the 5′ end of the RNA.

    Journal: The Journal of biological chemistry

    Article Title: Sequence, Distance, and Accessibility are Determinants of 5? End-Directed Cleavages by Retroviral RNases H *

    doi: 10.1074/jbc.M510504200

    Figure Lengend Snippet: Alignment of sequences flanking RNA 5′ end-directed cleavage sites recognized by HIV-1 RNase H ). In the center column, the sequence surrounding each cleavage site is given, with the location of the cleavage site represented as a gap. The right column gives the position of each cleavage site counting from the 5′ end of the RNA.

    Article Snippet: Enzymes and reagents —Recombinant HIV-1 reverse transcriptase was obtained from Worthington Biochemicals.

    Techniques: Sequencing

    Comparison of HIV-1 and M-MuLV RNase H 5′ end-directed cleavages in the sequences of RNAs Md1 - Md10 . The sequences of the 29-mer RNAs Md1 through Md10 are aligned by the RNA 5′ ends to compare the positions of 5′ end-directed cleavage sites. In each sequence, the extent of cleavage at a site is indicated as strong (large arrows) or medium (small arrows) for HIV-1 reverse transcriptase (above) or M-MuLV reverse transcriptase (below). As described in the Discussion, the range of the closest and furthest independent 5′ end-directed cleavage sites is indicated by the positions of the bordering nucleotides from the RNA 5′ end, the position of site G in substrates Md1 and Md7 is indicated, and the grey box highlights nucleotide positions +13 and +20 that include the range of distances where the 5′ end-directed cleavages occur.

    Journal: The Journal of biological chemistry

    Article Title: Sequence, Distance, and Accessibility are Determinants of 5? End-Directed Cleavages by Retroviral RNases H *

    doi: 10.1074/jbc.M510504200

    Figure Lengend Snippet: Comparison of HIV-1 and M-MuLV RNase H 5′ end-directed cleavages in the sequences of RNAs Md1 - Md10 . The sequences of the 29-mer RNAs Md1 through Md10 are aligned by the RNA 5′ ends to compare the positions of 5′ end-directed cleavage sites. In each sequence, the extent of cleavage at a site is indicated as strong (large arrows) or medium (small arrows) for HIV-1 reverse transcriptase (above) or M-MuLV reverse transcriptase (below). As described in the Discussion, the range of the closest and furthest independent 5′ end-directed cleavage sites is indicated by the positions of the bordering nucleotides from the RNA 5′ end, the position of site G in substrates Md1 and Md7 is indicated, and the grey box highlights nucleotide positions +13 and +20 that include the range of distances where the 5′ end-directed cleavages occur.

    Article Snippet: Enzymes and reagents —Recombinant HIV-1 reverse transcriptase was obtained from Worthington Biochemicals.

    Techniques: Sequencing

    Extent of cleavage and optimal distances for cleavage at sites F, G, and H in RNAs Md1 through Md10 by HIV-1 and M-MuLV reverse transcriptases . The amount of product generated by cleavage (% of total) at sites F, G, and H in the indicated substrates was determined for HIV-1 (A) or M-MuLV (B) reverse transcriptase. Data from the 1 min time points in three (A) or four (B) independent experiments with 5′ end-labeled RNAs were used to determine the amount of product that resulted from the cleavages at site F (gray bars), site G (black bars), or site H (white bars) (± S.D.). These same data were also used to analyze the optimal distance for cleavage of each site relative to the 5′ RNA ends for HIV-1 (C) or M-MuLV (D) reverse transcriptase. The amount of product generated by cleavage (% of total) for sites F (gray squares), G (black circles), or H (open triangles) is plotted as a function of the cleavage site distance in nucleotides from the 5′ end of each substrate.

    Journal: The Journal of biological chemistry

    Article Title: Sequence, Distance, and Accessibility are Determinants of 5? End-Directed Cleavages by Retroviral RNases H *

    doi: 10.1074/jbc.M510504200

    Figure Lengend Snippet: Extent of cleavage and optimal distances for cleavage at sites F, G, and H in RNAs Md1 through Md10 by HIV-1 and M-MuLV reverse transcriptases . The amount of product generated by cleavage (% of total) at sites F, G, and H in the indicated substrates was determined for HIV-1 (A) or M-MuLV (B) reverse transcriptase. Data from the 1 min time points in three (A) or four (B) independent experiments with 5′ end-labeled RNAs were used to determine the amount of product that resulted from the cleavages at site F (gray bars), site G (black bars), or site H (white bars) (± S.D.). These same data were also used to analyze the optimal distance for cleavage of each site relative to the 5′ RNA ends for HIV-1 (C) or M-MuLV (D) reverse transcriptase. The amount of product generated by cleavage (% of total) for sites F (gray squares), G (black circles), or H (open triangles) is plotted as a function of the cleavage site distance in nucleotides from the 5′ end of each substrate.

    Article Snippet: Enzymes and reagents —Recombinant HIV-1 reverse transcriptase was obtained from Worthington Biochemicals.

    Techniques: Generated, Labeling