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  • 99
    New England Biolabs dnase i digestion solution
    Dnase I Digestion Solution, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore triton x 100
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Triton X 100, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 65173 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    New England Biolabs triton x 100 new england biolabs
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Triton X 100 New England Biolabs, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    New England Biolabs triton x 100
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Triton X 100, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 93/100, based on 1109 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    new england biolabs triton x 100 solution
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Triton X 100 Solution, supplied by new england biolabs, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    New England Biolabs reaction buffer
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Reaction Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 2709 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    New England Biolabs digestion buffer
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Digestion Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 395 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs vanadyl ribonucleoside complex
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Vanadyl Ribonucleoside Complex, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 410 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    New England Biolabs taq polymerase
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Taq Polymerase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 9100 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    New England Biolabs lysis buffer
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Lysis Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1884 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    New England Biolabs mung bean reaction buffer
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Mung Bean Reaction Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    New England Biolabs a tailing solution
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    A Tailing Solution, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs oligo
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Oligo, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1103 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs solution
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Solution, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs ligation mix
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Ligation Mix, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 761 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs neb t 720 buffer
    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.
    Neb T 720 Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs lambda phosphatase
    Analysis of PFV Gag phosphorylation status in purified virus particles. PFV virions were produced by transient transfection of the four-component PFV vector system, containing the pcoPG4 variants denoted above each of the blots, into 293T cells. Viral particles were pelleted from cell-free tissue culture supernatants by ultracentrifugation through 20% sucrose and equal amounts of particle lysates separated by SDS-PAGE were blotted to nitrocellulose membranes. The phosphorylation status of the particle-associated Gag variants was determined by the corresponding antibodies specific for different phosphorylated amino acid motives as indicated. Data are representative of n = 4 independent experiments. (A) Schematic illustration of PFV Gag protein organization with highlighted putative T-P motifs and surrounding amino acids recognized when phosphorylated at the threonine residue by either the α-pT-P (orange letters) or α-Gag S-pT-P (blue letters) phosphopeptide-specific antibody. Solid vertical arrow: primary Gag processing site; dashed vertical arrows: secondary Gag processing sites; (B) Detection of the phosphorylated Thr-Pro (pT-P) motives in PFV Gag wt, iSTP and pmSTP virus particles (α-pT-P antiserum) and comparison with the total Gag content in the particle lysates (α-Gag). (C) Comparison of the pT-P phosphorylation status in the wt and T225A PFV particles in the absence (-) or presence (+) of the <t>Lambda</t> Phosphatase (λP) pretreatment of viral proteins. (D) Comparison of the PFV Gag-associated S-T-P motif phosphorylation status (α-Gag S-pT-P; detected with the corresponding PFV Gag-specific antibody) in virus preparations containing either the wt or the T225A Gag variant in the absence (-) or presence (+) of the λP pretreatment.
    Lambda Phosphatase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1378 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    New England Biolabs triton x100 solution
    Analysis of PFV Gag phosphorylation status in purified virus particles. PFV virions were produced by transient transfection of the four-component PFV vector system, containing the pcoPG4 variants denoted above each of the blots, into 293T cells. Viral particles were pelleted from cell-free tissue culture supernatants by ultracentrifugation through 20% sucrose and equal amounts of particle lysates separated by SDS-PAGE were blotted to nitrocellulose membranes. The phosphorylation status of the particle-associated Gag variants was determined by the corresponding antibodies specific for different phosphorylated amino acid motives as indicated. Data are representative of n = 4 independent experiments. (A) Schematic illustration of PFV Gag protein organization with highlighted putative T-P motifs and surrounding amino acids recognized when phosphorylated at the threonine residue by either the α-pT-P (orange letters) or α-Gag S-pT-P (blue letters) phosphopeptide-specific antibody. Solid vertical arrow: primary Gag processing site; dashed vertical arrows: secondary Gag processing sites; (B) Detection of the phosphorylated Thr-Pro (pT-P) motives in PFV Gag wt, iSTP and pmSTP virus particles (α-pT-P antiserum) and comparison with the total Gag content in the particle lysates (α-Gag). (C) Comparison of the pT-P phosphorylation status in the wt and T225A PFV particles in the absence (-) or presence (+) of the <t>Lambda</t> Phosphatase (λP) pretreatment of viral proteins. (D) Comparison of the PFV Gag-associated S-T-P motif phosphorylation status (α-Gag S-pT-P; detected with the corresponding PFV Gag-specific antibody) in virus preparations containing either the wt or the T225A Gag variant in the absence (-) or presence (+) of the λP pretreatment.
    Triton X100 Solution, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown.  B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown.  C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ).  IP , immunoprecipitation.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Stable Isotope Labeling by Amino Acids in Cell Culture and Differential Plasma Membrane Proteome Quantitation Identify New Substrates for the MARCH9 Transmembrane E3 Ligase *

    doi: 10.1074/mcp.M900174-MCP200

    Figure Lengend Snippet: Mechanism of substrate down-regulation. A , FcγRIIB or SLAM were co-transfected together with GFP-tagged wild-type or tryptophan to alanine mutant ( W/A ) MARCH9 into 293T cells and stained with antibodies specific for FcγRIIB or SLAM. The percentage of cells in each quadrant is shown. B , pulse-chase analysis of metabolically labeled HA-tagged SLAM in the presence or absence of MARCH9. HA-tagged SLAM-expressing 293T cells in the presence or absence of MARCH9 were [ 35 S]methionine-radiolabeled for 20 min and chased for the times indicated. Triton X-100 lysates were immunoprecipitated with HA-specific monoclonal antibody and treated with Endo H. Samples were analyzed by SDS-PAGE and autoradiography. The half-life ( t ½) of the Endo H-sensitive, immature form and the Endo H-resistant, mature form of SLAM is shown. C , Tsg101 siRNA-depleted 293T cells were co-transfected with SLAM and GFP-tagged MARCH9. SLAM and MARCH9 expression were analyzed by flow cytometry and compared with mock-depleted cells or cells transfected with tryptophan to alanine mutant MARCH9 ( W/A ). IP , immunoprecipitation.

    Article Snippet: The cells were lysed in 1% Triton X-100 and precleared twice with CL-4B Sepharose beads (Sigma-Aldrich), and HA-tagged SLAM was precipitated with the HA.11 monoclonal antibody (clone 16B12, Covance) and protein A-Sepharose for 1 h, washed three times with 0.5% Triton X-100 in PBS, eluted in sample buffer, and heated to 95 °C for 10 min. For endoglycosidase H (Endo H) digestion samples were supplemented with 250 units of Endo H (New England Biolabs) and incubated at 37 °C for 1 h.

    Techniques: Transfection, Mutagenesis, Staining, Pulse Chase, Metabolic Labelling, Labeling, Expressing, Immunoprecipitation, SDS Page, Autoradiography, Flow Cytometry, Cytometry

    Analysis of PFV Gag phosphorylation status in purified virus particles. PFV virions were produced by transient transfection of the four-component PFV vector system, containing the pcoPG4 variants denoted above each of the blots, into 293T cells. Viral particles were pelleted from cell-free tissue culture supernatants by ultracentrifugation through 20% sucrose and equal amounts of particle lysates separated by SDS-PAGE were blotted to nitrocellulose membranes. The phosphorylation status of the particle-associated Gag variants was determined by the corresponding antibodies specific for different phosphorylated amino acid motives as indicated. Data are representative of n = 4 independent experiments. (A) Schematic illustration of PFV Gag protein organization with highlighted putative T-P motifs and surrounding amino acids recognized when phosphorylated at the threonine residue by either the α-pT-P (orange letters) or α-Gag S-pT-P (blue letters) phosphopeptide-specific antibody. Solid vertical arrow: primary Gag processing site; dashed vertical arrows: secondary Gag processing sites; (B) Detection of the phosphorylated Thr-Pro (pT-P) motives in PFV Gag wt, iSTP and pmSTP virus particles (α-pT-P antiserum) and comparison with the total Gag content in the particle lysates (α-Gag). (C) Comparison of the pT-P phosphorylation status in the wt and T225A PFV particles in the absence (-) or presence (+) of the Lambda Phosphatase (λP) pretreatment of viral proteins. (D) Comparison of the PFV Gag-associated S-T-P motif phosphorylation status (α-Gag S-pT-P; detected with the corresponding PFV Gag-specific antibody) in virus preparations containing either the wt or the T225A Gag variant in the absence (-) or presence (+) of the λP pretreatment.

    Journal: PLoS Pathogens

    Article Title: Interactions of Prototype Foamy Virus Capsids with Host Cell Polo-Like Kinases Are Important for Efficient Viral DNA Integration

    doi: 10.1371/journal.ppat.1005860

    Figure Lengend Snippet: Analysis of PFV Gag phosphorylation status in purified virus particles. PFV virions were produced by transient transfection of the four-component PFV vector system, containing the pcoPG4 variants denoted above each of the blots, into 293T cells. Viral particles were pelleted from cell-free tissue culture supernatants by ultracentrifugation through 20% sucrose and equal amounts of particle lysates separated by SDS-PAGE were blotted to nitrocellulose membranes. The phosphorylation status of the particle-associated Gag variants was determined by the corresponding antibodies specific for different phosphorylated amino acid motives as indicated. Data are representative of n = 4 independent experiments. (A) Schematic illustration of PFV Gag protein organization with highlighted putative T-P motifs and surrounding amino acids recognized when phosphorylated at the threonine residue by either the α-pT-P (orange letters) or α-Gag S-pT-P (blue letters) phosphopeptide-specific antibody. Solid vertical arrow: primary Gag processing site; dashed vertical arrows: secondary Gag processing sites; (B) Detection of the phosphorylated Thr-Pro (pT-P) motives in PFV Gag wt, iSTP and pmSTP virus particles (α-pT-P antiserum) and comparison with the total Gag content in the particle lysates (α-Gag). (C) Comparison of the pT-P phosphorylation status in the wt and T225A PFV particles in the absence (-) or presence (+) of the Lambda Phosphatase (λP) pretreatment of viral proteins. (D) Comparison of the PFV Gag-associated S-T-P motif phosphorylation status (α-Gag S-pT-P; detected with the corresponding PFV Gag-specific antibody) in virus preparations containing either the wt or the T225A Gag variant in the absence (-) or presence (+) of the λP pretreatment.

    Article Snippet: Subsequently, half of the sample was digested for 1 h at 30°C with Lambda Phosphatase (NEB, P0753; 7.15 U/μl Lambda PP, 1% Triton X-100, 1 mM MnCl2 , 1x Lambda Phosphatase buffer) whereas the other half was mock digested prior to addition of protein sample buffer.

    Techniques: Purification, Produced, Transfection, Plasmid Preparation, SDS Page, Variant Assay