n biotinyl 1 2 dihexadecanoyl sn glycero 3 phosphoethanol amine Thermo Fisher Search Results


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    Crosslinking of COPII proteins and membrane lipids in the synthetic COPII vesicles generated from liposomes. Liposomes containing <t>NBD-PE</t> were incubated with COPII-coat proteins for 30 min at room temperature in the presence and absence of GMP-PNP. After incubation, the whole reaction mixture was incubated with various combinations of disuccinimidyl suberate (DSS, 100 μM final concentration) and NHS-biotin. After quenching the amine-reactive reagents, proteins in the incubation mixture were resolved by SDS/PAGE, and the NBD fluorescence of the proteins, biotinylation, and total protein was visualized as described in Materials and Methods . ( A ) NBD fluorescence represents NBD-PE <t>crosslinked</t> by disuccinimidyl suberate (DSS) to COPII proteins. ( B ) NHS-biotin labeling of reactive amino groups on all proteins in each sample. ( C ) Colloidal gold staining of all proteins in each sample. Sec31p* indicates a degradation product of Sec31p present in our preparation.
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    Crosslinking of COPII proteins and membrane lipids in the synthetic COPII vesicles generated from liposomes. Liposomes containing <t>NBD-PE</t> were incubated with COPII-coat proteins for 30 min at room temperature in the presence and absence of GMP-PNP. After incubation, the whole reaction mixture was incubated with various combinations of disuccinimidyl suberate (DSS, 100 μM final concentration) and NHS-biotin. After quenching the amine-reactive reagents, proteins in the incubation mixture were resolved by SDS/PAGE, and the NBD fluorescence of the proteins, biotinylation, and total protein was visualized as described in Materials and Methods . ( A ) NBD fluorescence represents NBD-PE <t>crosslinked</t> by disuccinimidyl suberate (DSS) to COPII proteins. ( B ) NHS-biotin labeling of reactive amino groups on all proteins in each sample. ( C ) Colloidal gold staining of all proteins in each sample. Sec31p* indicates a degradation product of Sec31p present in our preparation.
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    Crosslinking of COPII proteins and membrane lipids in the synthetic COPII vesicles generated from liposomes. Liposomes containing <t>NBD-PE</t> were incubated with COPII-coat proteins for 30 min at room temperature in the presence and absence of GMP-PNP. After incubation, the whole reaction mixture was incubated with various combinations of disuccinimidyl suberate (DSS, 100 μM final concentration) and NHS-biotin. After quenching the amine-reactive reagents, proteins in the incubation mixture were resolved by SDS/PAGE, and the NBD fluorescence of the proteins, biotinylation, and total protein was visualized as described in Materials and Methods . ( A ) NBD fluorescence represents NBD-PE <t>crosslinked</t> by disuccinimidyl suberate (DSS) to COPII proteins. ( B ) NHS-biotin labeling of reactive amino groups on all proteins in each sample. ( C ) Colloidal gold staining of all proteins in each sample. Sec31p* indicates a degradation product of Sec31p present in our preparation.
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    Crosslinking of COPII proteins and membrane lipids in the synthetic COPII vesicles generated from liposomes. Liposomes containing <t>NBD-PE</t> were incubated with COPII-coat proteins for 30 min at room temperature in the presence and absence of GMP-PNP. After incubation, the whole reaction mixture was incubated with various combinations of disuccinimidyl suberate (DSS, 100 μM final concentration) and NHS-biotin. After quenching the amine-reactive reagents, proteins in the incubation mixture were resolved by SDS/PAGE, and the NBD fluorescence of the proteins, biotinylation, and total protein was visualized as described in Materials and Methods . ( A ) NBD fluorescence represents NBD-PE <t>crosslinked</t> by disuccinimidyl suberate (DSS) to COPII proteins. ( B ) NHS-biotin labeling of reactive amino groups on all proteins in each sample. ( C ) Colloidal gold staining of all proteins in each sample. Sec31p* indicates a degradation product of Sec31p present in our preparation.
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    Image Search Results


    Crosslinking of COPII proteins and membrane lipids in the synthetic COPII vesicles generated from liposomes. Liposomes containing NBD-PE were incubated with COPII-coat proteins for 30 min at room temperature in the presence and absence of GMP-PNP. After incubation, the whole reaction mixture was incubated with various combinations of disuccinimidyl suberate (DSS, 100 μM final concentration) and NHS-biotin. After quenching the amine-reactive reagents, proteins in the incubation mixture were resolved by SDS/PAGE, and the NBD fluorescence of the proteins, biotinylation, and total protein was visualized as described in Materials and Methods . ( A ) NBD fluorescence represents NBD-PE crosslinked by disuccinimidyl suberate (DSS) to COPII proteins. ( B ) NHS-biotin labeling of reactive amino groups on all proteins in each sample. ( C ) Colloidal gold staining of all proteins in each sample. Sec31p* indicates a degradation product of Sec31p present in our preparation.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Surface structure of the COPII-coated vesicle

    doi: 10.1073/pnas.241522198

    Figure Lengend Snippet: Crosslinking of COPII proteins and membrane lipids in the synthetic COPII vesicles generated from liposomes. Liposomes containing NBD-PE were incubated with COPII-coat proteins for 30 min at room temperature in the presence and absence of GMP-PNP. After incubation, the whole reaction mixture was incubated with various combinations of disuccinimidyl suberate (DSS, 100 μM final concentration) and NHS-biotin. After quenching the amine-reactive reagents, proteins in the incubation mixture were resolved by SDS/PAGE, and the NBD fluorescence of the proteins, biotinylation, and total protein was visualized as described in Materials and Methods . ( A ) NBD fluorescence represents NBD-PE crosslinked by disuccinimidyl suberate (DSS) to COPII proteins. ( B ) NHS-biotin labeling of reactive amino groups on all proteins in each sample. ( C ) Colloidal gold staining of all proteins in each sample. Sec31p* indicates a degradation product of Sec31p present in our preparation.

    Article Snippet: The resulting solution was mixed with 2 μl of crosslinkers in a solution of dimethyl sulfoxide with or without NHS-biotin for 30 min on ice, and then the excess crosslinker was quenched by mixing 3 μl of 0.25 M Tris/1.9 M glycine, pH 8.2 and incubated at room temperature for 30 min. Proteins in this reaction were separated by SDS/PAGE and transferred to a polyvinylidene difluoride membrane, and the fluorescence of crosslinked NBD-PE was recorded by using a STORM860 image analyzer at a setting of 950 V. After recording, biotinylated proteins on the membrane were probed with a streptavidin-alkaline phosphatase conjugate (Pierce), and the activity of alkaline phosphatase was detected by using the Vistra ECF substrate (Amersham Pharmacia).

    Techniques: Generated, Incubation, Concentration Assay, SDS Page, Fluorescence, Labeling, Staining