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quaternary ammonium-strong anion (sax-q1) modified sepharose prepacked ion-exchange columns  (Bio-Rad)


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    Bio-Rad quaternary ammonium-strong anion (sax-q1) modified sepharose prepacked ion-exchange columns
    Quaternary Ammonium Strong Anion (Sax Q1) Modified Sepharose Prepacked Ion Exchange Columns, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/quaternary ammonium-strong anion (sax-q1) modified sepharose prepacked ion-exchange columns/product/Bio-Rad
    Average 90 stars, based on 1 article reviews
    quaternary ammonium-strong anion (sax-q1) modified sepharose prepacked ion-exchange columns - by Bioz Stars, 2026-04
    90/100 stars

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    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.
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    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