sodium pyrophosphate Search Results


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  • 99
    Thermo Fisher sodium pyrophosphate
    Sodium Pyrophosphate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 498 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore sodium pyrophosphate
    Sodium Pyrophosphate, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 4353 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore m sodium pyrophosphate
    M Sodium Pyrophosphate, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 426 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore adenosine 5 diphosphate sodium salt
    Adenosine 5 Diphosphate Sodium Salt, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 48 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fisher Scientific sodium pyrophosphate
    Sodium Pyrophosphate, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 93/100, based on 82 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore gdp
    Arl5b interacts with Ragulator through Lamtor1. HEK293T cells were used. a Arl5b, but not Arl1, specifically pulled down Lamtor1-GFP. Bead-immobilized GST-Arl5b or Arl1 was in vitro loaded with <t>GDP</t> or <t>GMPPNP</t> and subsequently incubated with cell lysates expressing GFP or Lamtor1-GFP. Pull-downs were analyzed by immuno-blotting GFP fusions. The loading of GST fusions were shown by Coomassie blue staining. 1 and 2 indicate Lamtor1-GFP and GFP band, respectively. b , c Arl5b-QL and -TN interact with Lamtor1-Myc in forward and reverse co-IPs. Cells co-expressing indicated tagged-proteins were incubated with indicated antibodies and IPs were immuno-blotted against indicated tags. Lamtor2-GFP and SNX3-Myc served as a positive and negative control, respectively. In b , 1 and 2 indicate Arl5b-(wt, QL or TN)-GFP and Lamtor2-GFP band, respectively. In c , 1–5 indicate IgG heavy chain, Arl5b-(wt, QL or TN)-GFP, Lamtor2-GFP, SNX3-Myc, and Lamtor1-Myc band, respectively. d Full length Lamtor1 is required for Arl5b–Lamtor1 interaction. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated fragments of Lamtor1, and pull-downs were analyzed by immuno-blotting GFP-fusions. * denotes the specific band. e Arl5-QL and -TN interact with Lamtor1 but not Lamtor2–5. Bead-immobilized GST-fusion was incubated with cell lysates expressing indicated Myc-tagged Lamtors and pull-downs were analyzed by immuno-blotting Myc-tagged proteins. Lamtor1-Str.-Myc, Lamtor1-G2A-Strep-Myc. f Arl5b-TN interacts with Ragulator through Lamtor1. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated Lamtors, and pull-downs were analyzed by immuno-blotting indicated tags. 1 and 2 indicate DMyc-Lamtor5 and DMyc-Lamtor4, respectively. g Arl5b-GMPPNP, -GDP, and guanine nucleotide empty form interact with Ragulator. Bead-immobilized GST-Arl5b was first loaded with GMPPNP or GDP or stripped off its bound guanine nucleotide by EDTA treatment. Beads were subsequently incubated with cell lysate, and pull-downs were analyzed by immuno-blotting endogenous Lamtor1–4. h Excess Arl5b-TN inhibits the interaction between Rag GTPases and Lamtor1. Cell lysate co-expressing Lamtor1-GFP, Flag-RagB-T54L, and HA-GST-RagC was IPed using anti-GFP antibody in the presence of 0.2 µM recombinant GST-Arl5b-TN or GST. Pull-downs were subsequently immuno-blotted for indicated tags
    Gdp, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 2520 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore guanosine 5 diphosphate sodium salt gdp
    Arl5b interacts with Ragulator through Lamtor1. HEK293T cells were used. a Arl5b, but not Arl1, specifically pulled down Lamtor1-GFP. Bead-immobilized GST-Arl5b or Arl1 was in vitro loaded with <t>GDP</t> or <t>GMPPNP</t> and subsequently incubated with cell lysates expressing GFP or Lamtor1-GFP. Pull-downs were analyzed by immuno-blotting GFP fusions. The loading of GST fusions were shown by Coomassie blue staining. 1 and 2 indicate Lamtor1-GFP and GFP band, respectively. b , c Arl5b-QL and -TN interact with Lamtor1-Myc in forward and reverse co-IPs. Cells co-expressing indicated tagged-proteins were incubated with indicated antibodies and IPs were immuno-blotted against indicated tags. Lamtor2-GFP and SNX3-Myc served as a positive and negative control, respectively. In b , 1 and 2 indicate Arl5b-(wt, QL or TN)-GFP and Lamtor2-GFP band, respectively. In c , 1–5 indicate IgG heavy chain, Arl5b-(wt, QL or TN)-GFP, Lamtor2-GFP, SNX3-Myc, and Lamtor1-Myc band, respectively. d Full length Lamtor1 is required for Arl5b–Lamtor1 interaction. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated fragments of Lamtor1, and pull-downs were analyzed by immuno-blotting GFP-fusions. * denotes the specific band. e Arl5-QL and -TN interact with Lamtor1 but not Lamtor2–5. Bead-immobilized GST-fusion was incubated with cell lysates expressing indicated Myc-tagged Lamtors and pull-downs were analyzed by immuno-blotting Myc-tagged proteins. Lamtor1-Str.-Myc, Lamtor1-G2A-Strep-Myc. f Arl5b-TN interacts with Ragulator through Lamtor1. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated Lamtors, and pull-downs were analyzed by immuno-blotting indicated tags. 1 and 2 indicate DMyc-Lamtor5 and DMyc-Lamtor4, respectively. g Arl5b-GMPPNP, -GDP, and guanine nucleotide empty form interact with Ragulator. Bead-immobilized GST-Arl5b was first loaded with GMPPNP or GDP or stripped off its bound guanine nucleotide by EDTA treatment. Beads were subsequently incubated with cell lysate, and pull-downs were analyzed by immuno-blotting endogenous Lamtor1–4. h Excess Arl5b-TN inhibits the interaction between Rag GTPases and Lamtor1. Cell lysate co-expressing Lamtor1-GFP, Flag-RagB-T54L, and HA-GST-RagC was IPed using anti-GFP antibody in the presence of 0.2 µM recombinant GST-Arl5b-TN or GST. Pull-downs were subsequently immuno-blotted for indicated tags
    Guanosine 5 Diphosphate Sodium Salt Gdp, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore sodium pyrophosphate tetrabasic decahydrate
    Arl5b interacts with Ragulator through Lamtor1. HEK293T cells were used. a Arl5b, but not Arl1, specifically pulled down Lamtor1-GFP. Bead-immobilized GST-Arl5b or Arl1 was in vitro loaded with <t>GDP</t> or <t>GMPPNP</t> and subsequently incubated with cell lysates expressing GFP or Lamtor1-GFP. Pull-downs were analyzed by immuno-blotting GFP fusions. The loading of GST fusions were shown by Coomassie blue staining. 1 and 2 indicate Lamtor1-GFP and GFP band, respectively. b , c Arl5b-QL and -TN interact with Lamtor1-Myc in forward and reverse co-IPs. Cells co-expressing indicated tagged-proteins were incubated with indicated antibodies and IPs were immuno-blotted against indicated tags. Lamtor2-GFP and SNX3-Myc served as a positive and negative control, respectively. In b , 1 and 2 indicate Arl5b-(wt, QL or TN)-GFP and Lamtor2-GFP band, respectively. In c , 1–5 indicate IgG heavy chain, Arl5b-(wt, QL or TN)-GFP, Lamtor2-GFP, SNX3-Myc, and Lamtor1-Myc band, respectively. d Full length Lamtor1 is required for Arl5b–Lamtor1 interaction. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated fragments of Lamtor1, and pull-downs were analyzed by immuno-blotting GFP-fusions. * denotes the specific band. e Arl5-QL and -TN interact with Lamtor1 but not Lamtor2–5. Bead-immobilized GST-fusion was incubated with cell lysates expressing indicated Myc-tagged Lamtors and pull-downs were analyzed by immuno-blotting Myc-tagged proteins. Lamtor1-Str.-Myc, Lamtor1-G2A-Strep-Myc. f Arl5b-TN interacts with Ragulator through Lamtor1. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated Lamtors, and pull-downs were analyzed by immuno-blotting indicated tags. 1 and 2 indicate DMyc-Lamtor5 and DMyc-Lamtor4, respectively. g Arl5b-GMPPNP, -GDP, and guanine nucleotide empty form interact with Ragulator. Bead-immobilized GST-Arl5b was first loaded with GMPPNP or GDP or stripped off its bound guanine nucleotide by EDTA treatment. Beads were subsequently incubated with cell lysate, and pull-downs were analyzed by immuno-blotting endogenous Lamtor1–4. h Excess Arl5b-TN inhibits the interaction between Rag GTPases and Lamtor1. Cell lysate co-expressing Lamtor1-GFP, Flag-RagB-T54L, and HA-GST-RagC was IPed using anti-GFP antibody in the presence of 0.2 µM recombinant GST-Arl5b-TN or GST. Pull-downs were subsequently immuno-blotted for indicated tags
    Sodium Pyrophosphate Tetrabasic Decahydrate, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore sodium pyrophosphate tetrabasic
    Arl5b interacts with Ragulator through Lamtor1. HEK293T cells were used. a Arl5b, but not Arl1, specifically pulled down Lamtor1-GFP. Bead-immobilized GST-Arl5b or Arl1 was in vitro loaded with <t>GDP</t> or <t>GMPPNP</t> and subsequently incubated with cell lysates expressing GFP or Lamtor1-GFP. Pull-downs were analyzed by immuno-blotting GFP fusions. The loading of GST fusions were shown by Coomassie blue staining. 1 and 2 indicate Lamtor1-GFP and GFP band, respectively. b , c Arl5b-QL and -TN interact with Lamtor1-Myc in forward and reverse co-IPs. Cells co-expressing indicated tagged-proteins were incubated with indicated antibodies and IPs were immuno-blotted against indicated tags. Lamtor2-GFP and SNX3-Myc served as a positive and negative control, respectively. In b , 1 and 2 indicate Arl5b-(wt, QL or TN)-GFP and Lamtor2-GFP band, respectively. In c , 1–5 indicate IgG heavy chain, Arl5b-(wt, QL or TN)-GFP, Lamtor2-GFP, SNX3-Myc, and Lamtor1-Myc band, respectively. d Full length Lamtor1 is required for Arl5b–Lamtor1 interaction. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated fragments of Lamtor1, and pull-downs were analyzed by immuno-blotting GFP-fusions. * denotes the specific band. e Arl5-QL and -TN interact with Lamtor1 but not Lamtor2–5. Bead-immobilized GST-fusion was incubated with cell lysates expressing indicated Myc-tagged Lamtors and pull-downs were analyzed by immuno-blotting Myc-tagged proteins. Lamtor1-Str.-Myc, Lamtor1-G2A-Strep-Myc. f Arl5b-TN interacts with Ragulator through Lamtor1. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated Lamtors, and pull-downs were analyzed by immuno-blotting indicated tags. 1 and 2 indicate DMyc-Lamtor5 and DMyc-Lamtor4, respectively. g Arl5b-GMPPNP, -GDP, and guanine nucleotide empty form interact with Ragulator. Bead-immobilized GST-Arl5b was first loaded with GMPPNP or GDP or stripped off its bound guanine nucleotide by EDTA treatment. Beads were subsequently incubated with cell lysate, and pull-downs were analyzed by immuno-blotting endogenous Lamtor1–4. h Excess Arl5b-TN inhibits the interaction between Rag GTPases and Lamtor1. Cell lysate co-expressing Lamtor1-GFP, Flag-RagB-T54L, and HA-GST-RagC was IPed using anti-GFP antibody in the presence of 0.2 µM recombinant GST-Arl5b-TN or GST. Pull-downs were subsequently immuno-blotted for indicated tags
    Sodium Pyrophosphate Tetrabasic, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck & Co sodium pyrophosphate
    Arl5b interacts with Ragulator through Lamtor1. HEK293T cells were used. a Arl5b, but not Arl1, specifically pulled down Lamtor1-GFP. Bead-immobilized GST-Arl5b or Arl1 was in vitro loaded with <t>GDP</t> or <t>GMPPNP</t> and subsequently incubated with cell lysates expressing GFP or Lamtor1-GFP. Pull-downs were analyzed by immuno-blotting GFP fusions. The loading of GST fusions were shown by Coomassie blue staining. 1 and 2 indicate Lamtor1-GFP and GFP band, respectively. b , c Arl5b-QL and -TN interact with Lamtor1-Myc in forward and reverse co-IPs. Cells co-expressing indicated tagged-proteins were incubated with indicated antibodies and IPs were immuno-blotted against indicated tags. Lamtor2-GFP and SNX3-Myc served as a positive and negative control, respectively. In b , 1 and 2 indicate Arl5b-(wt, QL or TN)-GFP and Lamtor2-GFP band, respectively. In c , 1–5 indicate IgG heavy chain, Arl5b-(wt, QL or TN)-GFP, Lamtor2-GFP, SNX3-Myc, and Lamtor1-Myc band, respectively. d Full length Lamtor1 is required for Arl5b–Lamtor1 interaction. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated fragments of Lamtor1, and pull-downs were analyzed by immuno-blotting GFP-fusions. * denotes the specific band. e Arl5-QL and -TN interact with Lamtor1 but not Lamtor2–5. Bead-immobilized GST-fusion was incubated with cell lysates expressing indicated Myc-tagged Lamtors and pull-downs were analyzed by immuno-blotting Myc-tagged proteins. Lamtor1-Str.-Myc, Lamtor1-G2A-Strep-Myc. f Arl5b-TN interacts with Ragulator through Lamtor1. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated Lamtors, and pull-downs were analyzed by immuno-blotting indicated tags. 1 and 2 indicate DMyc-Lamtor5 and DMyc-Lamtor4, respectively. g Arl5b-GMPPNP, -GDP, and guanine nucleotide empty form interact with Ragulator. Bead-immobilized GST-Arl5b was first loaded with GMPPNP or GDP or stripped off its bound guanine nucleotide by EDTA treatment. Beads were subsequently incubated with cell lysate, and pull-downs were analyzed by immuno-blotting endogenous Lamtor1–4. h Excess Arl5b-TN inhibits the interaction between Rag GTPases and Lamtor1. Cell lysate co-expressing Lamtor1-GFP, Flag-RagB-T54L, and HA-GST-RagC was IPed using anti-GFP antibody in the presence of 0.2 µM recombinant GST-Arl5b-TN or GST. Pull-downs were subsequently immuno-blotted for indicated tags
    Sodium Pyrophosphate, supplied by Merck & Co, used in various techniques. Bioz Stars score: 92/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore udp glcnac
    Mutagenesis of OGT to accommodate diazirine modification to <t>UDP-GlcNAc.</t> A , a model of human OGT (Protein Data Bank entry 4GZ5 ) complexed with UDP-GlcNDAz substrate shows that the diazirine from the N -acyl group is in close proximity to positions
    Udp Glcnac, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 423 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Avantor sodium pyrophosphate
    Mutagenesis of OGT to accommodate diazirine modification to <t>UDP-GlcNAc.</t> A , a model of human OGT (Protein Data Bank entry 4GZ5 ) complexed with UDP-GlcNDAz substrate shows that the diazirine from the N -acyl group is in close proximity to positions
    Sodium Pyrophosphate, supplied by Avantor, used in various techniques. Bioz Stars score: 93/100, based on 65 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Mallinckrodt sodium pyrophosphate
    Mutagenesis of OGT to accommodate diazirine modification to <t>UDP-GlcNAc.</t> A , a model of human OGT (Protein Data Bank entry 4GZ5 ) complexed with UDP-GlcNDAz substrate shows that the diazirine from the N -acyl group is in close proximity to positions
    Sodium Pyrophosphate, supplied by Mallinckrodt, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore α β methyleneadenosine 5 diphosphate aopcp
    Mutagenesis of OGT to accommodate diazirine modification to <t>UDP-GlcNAc.</t> A , a model of human OGT (Protein Data Bank entry 4GZ5 ) complexed with UDP-GlcNDAz substrate shows that the diazirine from the N -acyl group is in close proximity to positions
    α β Methyleneadenosine 5 Diphosphate Aopcp, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    apcp  (Tocris)
    95
    Tocris apcp
    Mutagenesis of OGT to accommodate diazirine modification to <t>UDP-GlcNAc.</t> A , a model of human OGT (Protein Data Bank entry 4GZ5 ) complexed with UDP-GlcNDAz substrate shows that the diazirine from the N -acyl group is in close proximity to positions
    Apcp, supplied by Tocris, used in various techniques. Bioz Stars score: 95/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Arl5b interacts with Ragulator through Lamtor1. HEK293T cells were used. a Arl5b, but not Arl1, specifically pulled down Lamtor1-GFP. Bead-immobilized GST-Arl5b or Arl1 was in vitro loaded with GDP or GMPPNP and subsequently incubated with cell lysates expressing GFP or Lamtor1-GFP. Pull-downs were analyzed by immuno-blotting GFP fusions. The loading of GST fusions were shown by Coomassie blue staining. 1 and 2 indicate Lamtor1-GFP and GFP band, respectively. b , c Arl5b-QL and -TN interact with Lamtor1-Myc in forward and reverse co-IPs. Cells co-expressing indicated tagged-proteins were incubated with indicated antibodies and IPs were immuno-blotted against indicated tags. Lamtor2-GFP and SNX3-Myc served as a positive and negative control, respectively. In b , 1 and 2 indicate Arl5b-(wt, QL or TN)-GFP and Lamtor2-GFP band, respectively. In c , 1–5 indicate IgG heavy chain, Arl5b-(wt, QL or TN)-GFP, Lamtor2-GFP, SNX3-Myc, and Lamtor1-Myc band, respectively. d Full length Lamtor1 is required for Arl5b–Lamtor1 interaction. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated fragments of Lamtor1, and pull-downs were analyzed by immuno-blotting GFP-fusions. * denotes the specific band. e Arl5-QL and -TN interact with Lamtor1 but not Lamtor2–5. Bead-immobilized GST-fusion was incubated with cell lysates expressing indicated Myc-tagged Lamtors and pull-downs were analyzed by immuno-blotting Myc-tagged proteins. Lamtor1-Str.-Myc, Lamtor1-G2A-Strep-Myc. f Arl5b-TN interacts with Ragulator through Lamtor1. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated Lamtors, and pull-downs were analyzed by immuno-blotting indicated tags. 1 and 2 indicate DMyc-Lamtor5 and DMyc-Lamtor4, respectively. g Arl5b-GMPPNP, -GDP, and guanine nucleotide empty form interact with Ragulator. Bead-immobilized GST-Arl5b was first loaded with GMPPNP or GDP or stripped off its bound guanine nucleotide by EDTA treatment. Beads were subsequently incubated with cell lysate, and pull-downs were analyzed by immuno-blotting endogenous Lamtor1–4. h Excess Arl5b-TN inhibits the interaction between Rag GTPases and Lamtor1. Cell lysate co-expressing Lamtor1-GFP, Flag-RagB-T54L, and HA-GST-RagC was IPed using anti-GFP antibody in the presence of 0.2 µM recombinant GST-Arl5b-TN or GST. Pull-downs were subsequently immuno-blotted for indicated tags

    Journal: Nature Communications

    Article Title: Amino acids stimulate the endosome-to-Golgi trafficking through Ragulator and small GTPase Arl5

    doi: 10.1038/s41467-018-07444-y

    Figure Lengend Snippet: Arl5b interacts with Ragulator through Lamtor1. HEK293T cells were used. a Arl5b, but not Arl1, specifically pulled down Lamtor1-GFP. Bead-immobilized GST-Arl5b or Arl1 was in vitro loaded with GDP or GMPPNP and subsequently incubated with cell lysates expressing GFP or Lamtor1-GFP. Pull-downs were analyzed by immuno-blotting GFP fusions. The loading of GST fusions were shown by Coomassie blue staining. 1 and 2 indicate Lamtor1-GFP and GFP band, respectively. b , c Arl5b-QL and -TN interact with Lamtor1-Myc in forward and reverse co-IPs. Cells co-expressing indicated tagged-proteins were incubated with indicated antibodies and IPs were immuno-blotted against indicated tags. Lamtor2-GFP and SNX3-Myc served as a positive and negative control, respectively. In b , 1 and 2 indicate Arl5b-(wt, QL or TN)-GFP and Lamtor2-GFP band, respectively. In c , 1–5 indicate IgG heavy chain, Arl5b-(wt, QL or TN)-GFP, Lamtor2-GFP, SNX3-Myc, and Lamtor1-Myc band, respectively. d Full length Lamtor1 is required for Arl5b–Lamtor1 interaction. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated fragments of Lamtor1, and pull-downs were analyzed by immuno-blotting GFP-fusions. * denotes the specific band. e Arl5-QL and -TN interact with Lamtor1 but not Lamtor2–5. Bead-immobilized GST-fusion was incubated with cell lysates expressing indicated Myc-tagged Lamtors and pull-downs were analyzed by immuno-blotting Myc-tagged proteins. Lamtor1-Str.-Myc, Lamtor1-G2A-Strep-Myc. f Arl5b-TN interacts with Ragulator through Lamtor1. Bead-immobilized GST-Arl5b-TN was incubated with cell lysates expressing indicated Lamtors, and pull-downs were analyzed by immuno-blotting indicated tags. 1 and 2 indicate DMyc-Lamtor5 and DMyc-Lamtor4, respectively. g Arl5b-GMPPNP, -GDP, and guanine nucleotide empty form interact with Ragulator. Bead-immobilized GST-Arl5b was first loaded with GMPPNP or GDP or stripped off its bound guanine nucleotide by EDTA treatment. Beads were subsequently incubated with cell lysate, and pull-downs were analyzed by immuno-blotting endogenous Lamtor1–4. h Excess Arl5b-TN inhibits the interaction between Rag GTPases and Lamtor1. Cell lysate co-expressing Lamtor1-GFP, Flag-RagB-T54L, and HA-GST-RagC was IPed using anti-GFP antibody in the presence of 0.2 µM recombinant GST-Arl5b-TN or GST. Pull-downs were subsequently immuno-blotted for indicated tags

    Article Snippet: GMPPNP (#G0635) and GDP (#G7127) were from Sigma-Aldrich.

    Techniques: In Vitro, Incubation, Expressing, Staining, Negative Control, Recombinant

    Kinetics of [Δ17]Arf1-Mg 2+ -GDP binding to Arno (383 RU) ( A ) and Arno4M (665 RU) ( B ) in the presence of BFA (100 μ m ) during the association phase. Shown are increasing concentrations of Arf1 were injected (50, 100, 200, 400, 800, and 1600

    Journal: The Journal of Biological Chemistry

    Article Title: Kinetics of Interaction between ADP-ribosylation Factor-1 (Arf1) and the Sec7 Domain of Arno Guanine Nucleotide Exchange Factor, Modulation by Allosteric Factors, and the Uncompetitive Inhibitor Brefeldin A

    doi: 10.1074/jbc.M112.391748

    Figure Lengend Snippet: Kinetics of [Δ17]Arf1-Mg 2+ -GDP binding to Arno (383 RU) ( A ) and Arno4M (665 RU) ( B ) in the presence of BFA (100 μ m ) during the association phase. Shown are increasing concentrations of Arf1 were injected (50, 100, 200, 400, 800, and 1600

    Article Snippet: BFA, GDP sodium salt, and GTP lithium salt were purchased from Sigma.

    Techniques: Binding Assay, Injection

    Complex formation detection in the presence of GDP or GTP. A , shown are representative sensorgrams of [Δ17]Arf1 binding at 200 n m on immobilized Arno or Arno4M with or without 2 μ m GDP in the injection buffer. B , shown is the effect of

    Journal: The Journal of Biological Chemistry

    Article Title: Kinetics of Interaction between ADP-ribosylation Factor-1 (Arf1) and the Sec7 Domain of Arno Guanine Nucleotide Exchange Factor, Modulation by Allosteric Factors, and the Uncompetitive Inhibitor Brefeldin A

    doi: 10.1074/jbc.M112.391748

    Figure Lengend Snippet: Complex formation detection in the presence of GDP or GTP. A , shown are representative sensorgrams of [Δ17]Arf1 binding at 200 n m on immobilized Arno or Arno4M with or without 2 μ m GDP in the injection buffer. B , shown is the effect of

    Article Snippet: BFA, GDP sodium salt, and GTP lithium salt were purchased from Sigma.

    Techniques: Binding Assay, Injection

    Top , shown is a ribbon representation of Arf1 and Arno structures at different steps of the GDP to GTP nucleotide exchange. Arf1 full-length or Δ17 truncated bound to Mg 2+ -GDP (PDA codes 2K5U and 1U81, respectively) and bound to Mg 2+ -GTP (PDA

    Journal: The Journal of Biological Chemistry

    Article Title: Kinetics of Interaction between ADP-ribosylation Factor-1 (Arf1) and the Sec7 Domain of Arno Guanine Nucleotide Exchange Factor, Modulation by Allosteric Factors, and the Uncompetitive Inhibitor Brefeldin A

    doi: 10.1074/jbc.M112.391748

    Figure Lengend Snippet: Top , shown is a ribbon representation of Arf1 and Arno structures at different steps of the GDP to GTP nucleotide exchange. Arf1 full-length or Δ17 truncated bound to Mg 2+ -GDP (PDA codes 2K5U and 1U81, respectively) and bound to Mg 2+ -GTP (PDA

    Article Snippet: BFA, GDP sodium salt, and GTP lithium salt were purchased from Sigma.

    Techniques:

    Interaction of Immobilized Arno and Arno4M with Arf1-Mg2+ -GDP in the Presence of BFA and GDP

    Journal: The Journal of Biological Chemistry

    Article Title: Kinetics of Interaction between ADP-ribosylation Factor-1 (Arf1) and the Sec7 Domain of Arno Guanine Nucleotide Exchange Factor, Modulation by Allosteric Factors, and the Uncompetitive Inhibitor Brefeldin A

    doi: 10.1074/jbc.M112.391748

    Figure Lengend Snippet: Interaction of Immobilized Arno and Arno4M with Arf1-Mg2+ -GDP in the Presence of BFA and GDP

    Article Snippet: BFA, GDP sodium salt, and GTP lithium salt were purchased from Sigma.

    Techniques:

    Impact of additional tags on protein activities and sensitivity to BFA. A , shown are the kinetics of GDP to GTP nucleotide exchange on [Δ17]Arf1 (1 μ m ) catalyzed by His-AviTags-Arno4M (0,2 μ m ) in the presence of Bodipy-GTP (1 μ

    Journal: The Journal of Biological Chemistry

    Article Title: Kinetics of Interaction between ADP-ribosylation Factor-1 (Arf1) and the Sec7 Domain of Arno Guanine Nucleotide Exchange Factor, Modulation by Allosteric Factors, and the Uncompetitive Inhibitor Brefeldin A

    doi: 10.1074/jbc.M112.391748

    Figure Lengend Snippet: Impact of additional tags on protein activities and sensitivity to BFA. A , shown are the kinetics of GDP to GTP nucleotide exchange on [Δ17]Arf1 (1 μ m ) catalyzed by His-AviTags-Arno4M (0,2 μ m ) in the presence of Bodipy-GTP (1 μ

    Article Snippet: BFA, GDP sodium salt, and GTP lithium salt were purchased from Sigma.

    Techniques:

    Interaction of Immobilized Arno and Arno4M with Arf1-Mg2+ -GDP in the Presence of BFA but No GDP

    Journal: The Journal of Biological Chemistry

    Article Title: Kinetics of Interaction between ADP-ribosylation Factor-1 (Arf1) and the Sec7 Domain of Arno Guanine Nucleotide Exchange Factor, Modulation by Allosteric Factors, and the Uncompetitive Inhibitor Brefeldin A

    doi: 10.1074/jbc.M112.391748

    Figure Lengend Snippet: Interaction of Immobilized Arno and Arno4M with Arf1-Mg2+ -GDP in the Presence of BFA but No GDP

    Article Snippet: BFA, GDP sodium salt, and GTP lithium salt were purchased from Sigma.

    Techniques:

    [Δ17]Arf1-Mg 2+ -GDP binding to Arno and Arno4M in the presence of BFA and GDP. Kinetics of [Δ17]Arf1-Mg 2+ -GDP binding to immobilized Arno (383 RU) ( A ) and Arno4M (355 RU) ( B ) in the presence of 2 μ m GDP and 100 μ m BFA during

    Journal: The Journal of Biological Chemistry

    Article Title: Kinetics of Interaction between ADP-ribosylation Factor-1 (Arf1) and the Sec7 Domain of Arno Guanine Nucleotide Exchange Factor, Modulation by Allosteric Factors, and the Uncompetitive Inhibitor Brefeldin A

    doi: 10.1074/jbc.M112.391748

    Figure Lengend Snippet: [Δ17]Arf1-Mg 2+ -GDP binding to Arno and Arno4M in the presence of BFA and GDP. Kinetics of [Δ17]Arf1-Mg 2+ -GDP binding to immobilized Arno (383 RU) ( A ) and Arno4M (355 RU) ( B ) in the presence of 2 μ m GDP and 100 μ m BFA during

    Article Snippet: BFA, GDP sodium salt, and GTP lithium salt were purchased from Sigma.

    Techniques: Binding Assay

    The GDP to GTP nucleotide exchange on Arf1 upon binding to Sec7 domain.

    Journal: The Journal of Biological Chemistry

    Article Title: Kinetics of Interaction between ADP-ribosylation Factor-1 (Arf1) and the Sec7 Domain of Arno Guanine Nucleotide Exchange Factor, Modulation by Allosteric Factors, and the Uncompetitive Inhibitor Brefeldin A

    doi: 10.1074/jbc.M112.391748

    Figure Lengend Snippet: The GDP to GTP nucleotide exchange on Arf1 upon binding to Sec7 domain.

    Article Snippet: BFA, GDP sodium salt, and GTP lithium salt were purchased from Sigma.

    Techniques: Binding Assay

    Mutagenesis of OGT to accommodate diazirine modification to UDP-GlcNAc. A , a model of human OGT (Protein Data Bank entry 4GZ5 ) complexed with UDP-GlcNDAz substrate shows that the diazirine from the N -acyl group is in close proximity to positions

    Journal: The Journal of Biological Chemistry

    Article Title: Enhanced Transfer of a Photocross-linking N-Acetylglucosamine (GlcNAc) Analog by an O-GlcNAc Transferase Mutant with Converted Substrate Specificity *

    doi: 10.1074/jbc.M115.667006

    Figure Lengend Snippet: Mutagenesis of OGT to accommodate diazirine modification to UDP-GlcNAc. A , a model of human OGT (Protein Data Bank entry 4GZ5 ) complexed with UDP-GlcNDAz substrate shows that the diazirine from the N -acyl group is in close proximity to positions

    Article Snippet: UDP-GlcNAc (Sigma, U4375, > 98% purity) and/or UDP-GlcNDAz were included at the concentrations indicated.

    Techniques: Mutagenesis, Modification

    OGT(C917A) prefers UDP-GlcNDAz to UDP-GlcNAc. Glycosylated CKII peptides produced using OGT(C917A). OGT(C917A) (1 μ m ) was incubated together with CKII peptide (100 μ m ) and 500 μ m UDP-GlcNAc, 500 μ m UDP-GlcNDAz, or a mixture

    Journal: The Journal of Biological Chemistry

    Article Title: Enhanced Transfer of a Photocross-linking N-Acetylglucosamine (GlcNAc) Analog by an O-GlcNAc Transferase Mutant with Converted Substrate Specificity *

    doi: 10.1074/jbc.M115.667006

    Figure Lengend Snippet: OGT(C917A) prefers UDP-GlcNDAz to UDP-GlcNAc. Glycosylated CKII peptides produced using OGT(C917A). OGT(C917A) (1 μ m ) was incubated together with CKII peptide (100 μ m ) and 500 μ m UDP-GlcNAc, 500 μ m UDP-GlcNDAz, or a mixture

    Article Snippet: UDP-GlcNAc (Sigma, U4375, > 98% purity) and/or UDP-GlcNDAz were included at the concentrations indicated.

    Techniques: Produced, Incubation

    OGT glycosylation reactions with natural and unnatural substrates. OGT transfers GlcNAc from the natural substrate, UDP-GlcNAc, to serine or threonine residues of substrate peptides, producing O -GlcNAc-modified peptides. To incorporate O -GlcNDAz on peptides,

    Journal: The Journal of Biological Chemistry

    Article Title: Enhanced Transfer of a Photocross-linking N-Acetylglucosamine (GlcNAc) Analog by an O-GlcNAc Transferase Mutant with Converted Substrate Specificity *

    doi: 10.1074/jbc.M115.667006

    Figure Lengend Snippet: OGT glycosylation reactions with natural and unnatural substrates. OGT transfers GlcNAc from the natural substrate, UDP-GlcNAc, to serine or threonine residues of substrate peptides, producing O -GlcNAc-modified peptides. To incorporate O -GlcNDAz on peptides,

    Article Snippet: UDP-GlcNAc (Sigma, U4375, > 98% purity) and/or UDP-GlcNDAz were included at the concentrations indicated.

    Techniques: Modification

    OGT(C917A) yields increased peptide cross-linking in vitro . A , biotinylated CKII peptide was glycosylated by wtOGT or OGT(C917A) using UDP-GlcNAc alone (+ NAc ), UDP-GlcNDAz alone (+ DAz ), or an equimolar mixture of UDP-GlcNAc and UDP-GlcNDAz (+ NAc +

    Journal: The Journal of Biological Chemistry

    Article Title: Enhanced Transfer of a Photocross-linking N-Acetylglucosamine (GlcNAc) Analog by an O-GlcNAc Transferase Mutant with Converted Substrate Specificity *

    doi: 10.1074/jbc.M115.667006

    Figure Lengend Snippet: OGT(C917A) yields increased peptide cross-linking in vitro . A , biotinylated CKII peptide was glycosylated by wtOGT or OGT(C917A) using UDP-GlcNAc alone (+ NAc ), UDP-GlcNDAz alone (+ DAz ), or an equimolar mixture of UDP-GlcNAc and UDP-GlcNDAz (+ NAc +

    Article Snippet: UDP-GlcNAc (Sigma, U4375, > 98% purity) and/or UDP-GlcNDAz were included at the concentrations indicated.

    Techniques: In Vitro

    wtOGT and OGT(C917A) have reversed nucleotide sugar specificities. A , initial rates of UDP production by wtOGT with various concentrations of UDP-GlcNAc (0.3, 1, 3, 10, and 30 μ m ). B , initial rates of UDP production by wtOGT with various concentrations

    Journal: The Journal of Biological Chemistry

    Article Title: Enhanced Transfer of a Photocross-linking N-Acetylglucosamine (GlcNAc) Analog by an O-GlcNAc Transferase Mutant with Converted Substrate Specificity *

    doi: 10.1074/jbc.M115.667006

    Figure Lengend Snippet: wtOGT and OGT(C917A) have reversed nucleotide sugar specificities. A , initial rates of UDP production by wtOGT with various concentrations of UDP-GlcNAc (0.3, 1, 3, 10, and 30 μ m ). B , initial rates of UDP production by wtOGT with various concentrations

    Article Snippet: UDP-GlcNAc (Sigma, U4375, > 98% purity) and/or UDP-GlcNDAz were included at the concentrations indicated.

    Techniques:

    wtOGT prefers UDP-GlcNAc to UDP-GlcNDAz. Glycosylated CKII peptides produced using wtOGT. Wild-type OGT (1 μ m ) was incubated together with CKII peptide (100 μ m ) and 500 μ m UDP-GlcNAc, 500 μ m UDP-GlcNDAz, or a mixture of

    Journal: The Journal of Biological Chemistry

    Article Title: Enhanced Transfer of a Photocross-linking N-Acetylglucosamine (GlcNAc) Analog by an O-GlcNAc Transferase Mutant with Converted Substrate Specificity *

    doi: 10.1074/jbc.M115.667006

    Figure Lengend Snippet: wtOGT prefers UDP-GlcNAc to UDP-GlcNDAz. Glycosylated CKII peptides produced using wtOGT. Wild-type OGT (1 μ m ) was incubated together with CKII peptide (100 μ m ) and 500 μ m UDP-GlcNAc, 500 μ m UDP-GlcNDAz, or a mixture of

    Article Snippet: UDP-GlcNAc (Sigma, U4375, > 98% purity) and/or UDP-GlcNDAz were included at the concentrations indicated.

    Techniques: Produced, Incubation