storage g 150 buffer Search Results


superose 6  (GE Healthcare)
94
GE Healthcare superose 6
(A) All splitting factors were purified from E. coli in a three-step process after lysis; differential precipitation at 65°C removed most host proteins. In a second purification step, ABCE1 was isolated via a C-terminal His 6 affinity tag by IMAC. ABCE1 with disassembled FeS clusters and most degradation products were removed by subsequent AIEX. (B) Purified ABCE1 was analyzed by SDS–PAGE (12.5%, Coomassie staining). Some of the mutants show degradation products. (C) In SEC, all ABCE1 variants eluted in a single peak as seen by absorption at 280 nm (blue). Additional absorption at 410 nm (brown) demonstrates an assembled iron-sulfur cluster. SEC was performed in 20 mM Tris, pH 7.5, 150 mM NaCl, 5 mM MgCl 2 , and 1 mM DTT on a <t>Superose</t> <t>6</t> 2.4 ml analytical grade column (GE Healthcare) applying 20–30 μg of protein.
Superose 6, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/storage+g+150+buffer/pmc06124641-191-10-12?v=GE+Healthcare
Average 94 stars, based on 1 article reviews
superose 6 - by Bioz Stars, 2026-07
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storage g 150 buffer  (Bio-Rad)
98
Bio-Rad storage g 150 buffer
(A) All splitting factors were purified from E. coli in a three-step process after lysis; differential precipitation at 65°C removed most host proteins. In a second purification step, ABCE1 was isolated via a C-terminal His 6 affinity tag by IMAC. ABCE1 with disassembled FeS clusters and most degradation products were removed by subsequent AIEX. (B) Purified ABCE1 was analyzed by SDS–PAGE (12.5%, Coomassie staining). Some of the mutants show degradation products. (C) In SEC, all ABCE1 variants eluted in a single peak as seen by absorption at 280 nm (blue). Additional absorption at 410 nm (brown) demonstrates an assembled iron-sulfur cluster. SEC was performed in 20 mM Tris, pH 7.5, 150 mM NaCl, 5 mM MgCl 2 , and 1 mM DTT on a <t>Superose</t> <t>6</t> 2.4 ml analytical grade column (GE Healthcare) applying 20–30 μg of protein.
Storage G 150 Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/storage+g+150+buffer/pmc06124641-176-8-33?v=Bio-Rad
Average 98 stars, based on 1 article reviews
storage g 150 buffer - by Bioz Stars, 2026-07
98/100 stars
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(A) All splitting factors were purified from E. coli in a three-step process after lysis; differential precipitation at 65°C removed most host proteins. In a second purification step, ABCE1 was isolated via a C-terminal His 6 affinity tag by IMAC. ABCE1 with disassembled FeS clusters and most degradation products were removed by subsequent AIEX. (B) Purified ABCE1 was analyzed by SDS–PAGE (12.5%, Coomassie staining). Some of the mutants show degradation products. (C) In SEC, all ABCE1 variants eluted in a single peak as seen by absorption at 280 nm (blue). Additional absorption at 410 nm (brown) demonstrates an assembled iron-sulfur cluster. SEC was performed in 20 mM Tris, pH 7.5, 150 mM NaCl, 5 mM MgCl 2 , and 1 mM DTT on a Superose 6 2.4 ml analytical grade column (GE Healthcare) applying 20–30 μg of protein.

Journal: Life Science Alliance

Article Title: Ribosome recycling is coordinated by processive events in two asymmetric ATP sites of ABCE1

doi: 10.26508/lsa.201800095

Figure Lengend Snippet: (A) All splitting factors were purified from E. coli in a three-step process after lysis; differential precipitation at 65°C removed most host proteins. In a second purification step, ABCE1 was isolated via a C-terminal His 6 affinity tag by IMAC. ABCE1 with disassembled FeS clusters and most degradation products were removed by subsequent AIEX. (B) Purified ABCE1 was analyzed by SDS–PAGE (12.5%, Coomassie staining). Some of the mutants show degradation products. (C) In SEC, all ABCE1 variants eluted in a single peak as seen by absorption at 280 nm (blue). Additional absorption at 410 nm (brown) demonstrates an assembled iron-sulfur cluster. SEC was performed in 20 mM Tris, pH 7.5, 150 mM NaCl, 5 mM MgCl 2 , and 1 mM DTT on a Superose 6 2.4 ml analytical grade column (GE Healthcare) applying 20–30 μg of protein.

Article Snippet: All variants of ABCE1 were additionally run on a 2.4-ml Superose 6 (GE Healthcare) on an Äkta Ettan Chromatography System (GE Healthcare) at 4°C in Storage-G 150 buffer without glycerol recording absorption at 280 and 410 nm to analyze the integrity of the FeS clusters ( ).

Techniques: Purification, Lysis, Isolation, SDS Page, Staining