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gag abe  (Addgene inc)


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    Addgene inc gag abe
    Gag Abe, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gag abe/product/Addgene inc
    Average 92 stars, based on 12 article reviews
    gag abe - by Bioz Stars, 2026-03
    92/100 stars

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    ( A to C ) Gag processing, Env expression, and incorporation. (A) Cell and virion-associated proteins derived from 293 T cells transfected with WT or MA-mutant pNL4-3 molecular clones were probed with anti-Gag Ab and anti-Env (gp41) antibody (Ab). (B) Virion-associated proteins were probed with <t>anti-p17</t> (MA) polyclonal Ab. Representative Western blots from three independent experiments are shown. (C) Quantification of p17 monomer/dimer/trimer levels from Western blots in (B). The data are shown as means ± SEM from three independent experiments with statistical significance indicated (* P < 0.05; Student’s t test). ( D and E ) Membrane stripping assay using the indicated concentration of NP-40. (D) Representative Western blots from three experiments. (E) Quantification of p17 monomer levels from Western blots in (D), indicating the % of p17 retained following detergent treatment relative to the amount present in the absence of detergent. The data are shown as means ± SEM from three independent experiments with statistical significance indicated (* P < 0.05; Student’s t test). ( F ) Sedimentation analysis in a 10 to 70% sucrose gradient after stripping the viral membrane with 0.075% NP-40. Representative Western blots from three independent experiments are shown. ( G ) Sedimentation analysis in 3 to 60% OptiPrep gradient after stripping the viral membrane with 1% Triton X-100 (TX-100). Representative Western blots from three independent experiments are shown. The Western blots of the gradient fractions were analyzed using anti-Gag Ab for both the WT and mutant MA. P, pellet fraction. The core fraction highlighted in red was determined by RT assay (fig. S1B). ( H and I ) Quantification of p24 (H) and p17 (I) monomer levels from Western blots in (G). The data are shown as means ± SEM from three independent experiments.
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    ( A to C ) Gag processing, Env expression, and incorporation. (A) Cell and virion-associated proteins derived from 293 T cells transfected with WT or MA-mutant pNL4-3 molecular clones were probed with anti-Gag Ab and anti-Env (gp41) antibody (Ab). (B) Virion-associated proteins were probed with <t>anti-p17</t> (MA) polyclonal Ab. Representative Western blots from three independent experiments are shown. (C) Quantification of p17 monomer/dimer/trimer levels from Western blots in (B). The data are shown as means ± SEM from three independent experiments with statistical significance indicated (* P < 0.05; Student’s t test). ( D and E ) Membrane stripping assay using the indicated concentration of NP-40. (D) Representative Western blots from three experiments. (E) Quantification of p17 monomer levels from Western blots in (D), indicating the % of p17 retained following detergent treatment relative to the amount present in the absence of detergent. The data are shown as means ± SEM from three independent experiments with statistical significance indicated (* P < 0.05; Student’s t test). ( F ) Sedimentation analysis in a 10 to 70% sucrose gradient after stripping the viral membrane with 0.075% NP-40. Representative Western blots from three independent experiments are shown. ( G ) Sedimentation analysis in 3 to 60% OptiPrep gradient after stripping the viral membrane with 1% Triton X-100 (TX-100). Representative Western blots from three independent experiments are shown. The Western blots of the gradient fractions were analyzed using anti-Gag Ab for both the WT and mutant MA. P, pellet fraction. The core fraction highlighted in red was determined by RT assay (fig. S1B). ( H and I ) Quantification of p24 (H) and p17 (I) monomer levels from Western blots in (G). The data are shown as means ± SEM from three independent experiments.
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    Image Search Results


    ( A to C ) Gag processing, Env expression, and incorporation. (A) Cell and virion-associated proteins derived from 293 T cells transfected with WT or MA-mutant pNL4-3 molecular clones were probed with anti-Gag Ab and anti-Env (gp41) antibody (Ab). (B) Virion-associated proteins were probed with anti-p17 (MA) polyclonal Ab. Representative Western blots from three independent experiments are shown. (C) Quantification of p17 monomer/dimer/trimer levels from Western blots in (B). The data are shown as means ± SEM from three independent experiments with statistical significance indicated (* P < 0.05; Student’s t test). ( D and E ) Membrane stripping assay using the indicated concentration of NP-40. (D) Representative Western blots from three experiments. (E) Quantification of p17 monomer levels from Western blots in (D), indicating the % of p17 retained following detergent treatment relative to the amount present in the absence of detergent. The data are shown as means ± SEM from three independent experiments with statistical significance indicated (* P < 0.05; Student’s t test). ( F ) Sedimentation analysis in a 10 to 70% sucrose gradient after stripping the viral membrane with 0.075% NP-40. Representative Western blots from three independent experiments are shown. ( G ) Sedimentation analysis in 3 to 60% OptiPrep gradient after stripping the viral membrane with 1% Triton X-100 (TX-100). Representative Western blots from three independent experiments are shown. The Western blots of the gradient fractions were analyzed using anti-Gag Ab for both the WT and mutant MA. P, pellet fraction. The core fraction highlighted in red was determined by RT assay (fig. S1B). ( H and I ) Quantification of p24 (H) and p17 (I) monomer levels from Western blots in (G). The data are shown as means ± SEM from three independent experiments.

    Journal: Science Advances

    Article Title: Structural maturation of the matrix lattice is not required for HIV-1 particle infectivity

    doi: 10.1126/sciadv.adv4356

    Figure Lengend Snippet: ( A to C ) Gag processing, Env expression, and incorporation. (A) Cell and virion-associated proteins derived from 293 T cells transfected with WT or MA-mutant pNL4-3 molecular clones were probed with anti-Gag Ab and anti-Env (gp41) antibody (Ab). (B) Virion-associated proteins were probed with anti-p17 (MA) polyclonal Ab. Representative Western blots from three independent experiments are shown. (C) Quantification of p17 monomer/dimer/trimer levels from Western blots in (B). The data are shown as means ± SEM from three independent experiments with statistical significance indicated (* P < 0.05; Student’s t test). ( D and E ) Membrane stripping assay using the indicated concentration of NP-40. (D) Representative Western blots from three experiments. (E) Quantification of p17 monomer levels from Western blots in (D), indicating the % of p17 retained following detergent treatment relative to the amount present in the absence of detergent. The data are shown as means ± SEM from three independent experiments with statistical significance indicated (* P < 0.05; Student’s t test). ( F ) Sedimentation analysis in a 10 to 70% sucrose gradient after stripping the viral membrane with 0.075% NP-40. Representative Western blots from three independent experiments are shown. ( G ) Sedimentation analysis in 3 to 60% OptiPrep gradient after stripping the viral membrane with 1% Triton X-100 (TX-100). Representative Western blots from three independent experiments are shown. The Western blots of the gradient fractions were analyzed using anti-Gag Ab for both the WT and mutant MA. P, pellet fraction. The core fraction highlighted in red was determined by RT assay (fig. S1B). ( H and I ) Quantification of p24 (H) and p17 (I) monomer levels from Western blots in (G). The data are shown as means ± SEM from three independent experiments.

    Article Snippet: Additionally, a polyclonal anti-Gag p17 Ab (PAB1178) was obtained from Abnova.

    Techniques: Expressing, Derivative Assay, Transfection, Mutagenesis, Clone Assay, Western Blot, Membrane, Stripping Membranes, Concentration Assay, Sedimentation