prepacked anion exchanger column Search Results


prepacked high q ion exchange column  (Bio-Rad)
88
Bio-Rad prepacked high q ion exchange column
Prepacked High Q Ion Exchange Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cationexchange chromatography  (Bio-Rad)
99
Bio-Rad cationexchange chromatography
Cationexchange Chromatography, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cation exchange resin  (Bio-Rad)
93
Bio-Rad cation exchange resin
Cation Exchange Resin, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cation exchange resin - by Bioz Stars, 2026-08
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buffer exchange prepacked column pd 10  (Cytiva Europe)
96
Cytiva Europe buffer exchange prepacked column pd 10
Buffer Exchange Prepacked Column Pd 10, supplied by Cytiva Europe, 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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prepacked q sepharose anion exchange column  (Cytiva Europe)
96
Cytiva Europe 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 Cytiva Europe, 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
prepacked q sepharose anion exchange column - by Bioz Stars, 2026-08
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size exclusion hiload 16 600 superdex column  (Cytiva Europe)
93
Cytiva Europe size exclusion hiload 16 600 superdex 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.
Size Exclusion Hiload 16 600 Superdex Column, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
size exclusion hiload 16 600 superdex column - by Bioz Stars, 2026-08
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uno s6 prepacked monolith cation exchange column  (Bio-Rad)
93
Bio-Rad uno s6 prepacked monolith cation 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.
Uno S6 Prepacked Monolith Cation Exchange Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
uno s6 prepacked monolith cation exchange column - by Bioz Stars, 2026-08
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ion exchange column  (Cytiva Europe)
96
Cytiva Europe ion 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.
Ion Exchange Column, supplied by Cytiva Europe, 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
ion exchange column - by Bioz Stars, 2026-08
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poly prep prepacked ion exchange columns  (Bio-Rad)
96
Bio-Rad poly prep prepacked ion exchange columns
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.
Poly Prep Prepacked Ion Exchange Columns, supplied by Bio-Rad, 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
poly prep prepacked ion exchange columns - by Bioz Stars, 2026-08
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strong anion exchanger  (Cytiva Europe)
97
Cytiva Europe strong anion exchanger
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.
Strong Anion Exchanger, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 97 stars, based on 1 article reviews
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prepacked mono s cation exchange fplc column  (Danaher Inc)
86
Danaher Inc prepacked mono s cation exchange fplc 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 Mono S Cation Exchange Fplc Column, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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buffer exchange prepacked column econo pac 10dg  (Bio-Rad)
96
Bio-Rad buffer exchange prepacked column econo pac 10dg
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.
Buffer Exchange Prepacked Column Econo Pac 10dg, supplied by Bio-Rad, 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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buffer exchange prepacked column econo pac 10dg - by Bioz Stars, 2026-08
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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