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prepacked anion exchanger column  (GE Healthcare)


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    Structured Review

    GE Healthcare prepacked anion exchanger column
    Prepacked Anion Exchanger Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 96/100, based on 752 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/prepacked+anion+exchanger+column/pmc04689727-73-15-43?v=GE+Healthcare
    Average 96 stars, based on 752 article reviews
    prepacked anion exchanger column - by Bioz Stars, 2026-07
    96/100 stars

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    GE Healthcare prepacked q sepharose anion exchange column
    Purification of 21-kDa protein. 10 mg of venom was separated by <t>Q-Sepharose</t> ion-exchange chromatography ( A ), and the selected fractions (9–26) were analyzed by 10% non-reducing SDS-PAGE ( B ). The partially purified protein at 21 kDa is indicated by arrows . Selected fractions were further separated by Superdex 75 gel filtration chromatography ( C ) and analyzed by 10% non-reducing SDS-PAGE ( D ). The purified venom protein was analyzed under non-reducing and reducing conditions by 4–20% gradient SDS-PAGE ( E ) and 10–20% Tris-Tricine gels ( F ). The cross-reactivity of antibody raised against the snaclecs of E. ocellatus with the purified protein was analyzed by immunoblot (obtained from a Tris-Tricine gel under non-reducing ( left ) and reducing ( right ) conditions) ( G ). mAU , milliabsorbance units; MW , molecular weight.
    Prepacked Q Sepharose Anion Exchange Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 96 stars, based on 1 article reviews
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    96
    GE Healthcare prepacked anion exchange column
    Purification of 21-kDa protein. 10 mg of venom was separated by <t>Q-Sepharose</t> ion-exchange chromatography ( A ), and the selected fractions (9–26) were analyzed by 10% non-reducing SDS-PAGE ( B ). The partially purified protein at 21 kDa is indicated by arrows . Selected fractions were further separated by Superdex 75 gel filtration chromatography ( C ) and analyzed by 10% non-reducing SDS-PAGE ( D ). The purified venom protein was analyzed under non-reducing and reducing conditions by 4–20% gradient SDS-PAGE ( E ) and 10–20% Tris-Tricine gels ( F ). The cross-reactivity of antibody raised against the snaclecs of E. ocellatus with the purified protein was analyzed by immunoblot (obtained from a Tris-Tricine gel under non-reducing ( left ) and reducing ( right ) conditions) ( G ). mAU , milliabsorbance units; MW , molecular weight.
    Prepacked Anion Exchange Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/prepacked+anion+exchanger+column/pm21493682-57-6-13?v=GE+Healthcare
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    Image Search Results


    Purification of 21-kDa protein. 10 mg of venom was separated by Q-Sepharose ion-exchange chromatography ( A ), and the selected fractions (9–26) were analyzed by 10% non-reducing SDS-PAGE ( B ). The partially purified protein at 21 kDa is indicated by arrows . Selected fractions were further separated by Superdex 75 gel filtration chromatography ( C ) and analyzed by 10% non-reducing SDS-PAGE ( D ). The purified venom protein was analyzed under non-reducing and reducing conditions by 4–20% gradient SDS-PAGE ( E ) and 10–20% Tris-Tricine gels ( F ). The cross-reactivity of antibody raised against the snaclecs of E. ocellatus with the purified protein was analyzed by immunoblot (obtained from a Tris-Tricine gel under non-reducing ( left ) and reducing ( right ) conditions) ( G ). mAU , milliabsorbance units; MW , molecular weight.

    Journal: The Journal of Biological Chemistry

    Article Title: Rhinocetin, a Venom-derived Integrin-specific Antagonist Inhibits Collagen-induced Platelet and Endothelial Cell Functions *

    doi: 10.1074/jbc.M112.381483

    Figure Lengend Snippet: Purification of 21-kDa protein. 10 mg of venom was separated by Q-Sepharose ion-exchange chromatography ( A ), and the selected fractions (9–26) were analyzed by 10% non-reducing SDS-PAGE ( B ). The partially purified protein at 21 kDa is indicated by arrows . Selected fractions were further separated by Superdex 75 gel filtration chromatography ( C ) and analyzed by 10% non-reducing SDS-PAGE ( D ). The purified venom protein was analyzed under non-reducing and reducing conditions by 4–20% gradient SDS-PAGE ( E ) and 10–20% Tris-Tricine gels ( F ). The cross-reactivity of antibody raised against the snaclecs of E. ocellatus with the purified protein was analyzed by immunoblot (obtained from a Tris-Tricine gel under non-reducing ( left ) and reducing ( right ) conditions) ( G ). mAU , milliabsorbance units; MW , molecular weight.

    Article Snippet: The clear venom sample was loaded on to a 1-ml prepacked Q-Sepharose anion-exchange column (GE Healthcare).

    Techniques: Purification, Ion Exchange Chromatography, SDS Page, Filtration, Chromatography, Western Blot, Molecular Weight