c8 column Search Results


93
MACHEREY NAGEL macherey nagel nucleodur c8 gravity column
Macherey Nagel Nucleodur C8 Gravity Column, supplied by MACHEREY NAGEL, 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
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Teledyne LABS silica gel chromatography
Silica Gel Chromatography, supplied by Teledyne LABS, 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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MACHEREY NAGEL c8 ec column
C8 Ec Column, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c8+column/EC+HPLC+column+(analytical)%2C+NUCLEODUR+100-3+C8+ec/pmc12421966-190-25-28
Average 93 stars, based on 1 article reviews
c8 ec column - by Bioz Stars, 2026-10
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MACHEREY NAGEL nucleodur c8 gravity column
Nucleodur C8 Gravity Column, supplied by MACHEREY NAGEL, 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
nucleodur c8 gravity column - by Bioz Stars, 2026-10
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85
MACHEREY NAGEL nucleosil 120 5 c8 column
Nucleosil 120 5 C8 Column, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 85 stars, based on 1 article reviews
nucleosil 120 5 c8 column - by Bioz Stars, 2026-10
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MACHEREY NAGEL nagel chromabond c8 spe columns
Nagel Chromabond C8 Spe Columns, supplied by MACHEREY NAGEL, 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
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MACHEREY NAGEL nucleosil c8 column
Nucleosil C8 Column, supplied by MACHEREY NAGEL, 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
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MACHEREY NAGEL c8 hd column
C8 Hd Column, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
MACHEREY NAGEL nucleosil 300 5
Purification of the native protease. A, size exclusion chromatography of 100 μl of C. salei venom in 100 mm NH4OAc, pH 5.0, on a Superdex 75 HR column. The proteolytic activity of collected fractions against the PQM substrate (red dashed line; DABCYL-PFFENEQARKDDKN-Glu(EDANS)-NH2) and the iPQM substrate (green dashed line; DABCYL-FYPSQRSETD-Glu(EDANS)-NH2) is given in percentage of degraded substrate. B, cation exchange chromatography of size exclusion chromatography peak 2 on a MiniS PE column equilibrated with 50 mm NH4OAc, pH 5.0. C, subsequent RP-HPLC separation of cation exchange chromatography peak 5 on a <t>Nucleosil</t> 300–5, C4 column equilibrated with 0.05% (v/v) TFA in water. D, SDS-PAGE (8–25%) of C. salei venom and pooled active fractions of each purification step. Bands referred to in the text are lettered.
Nucleosil 300 5, supplied by MACHEREY NAGEL, 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
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MACHEREY NAGEL guard column ec 4 3 nucleosil 120 3 c8
Purification of the native protease. A, size exclusion chromatography of 100 μl of C. salei venom in 100 mm NH4OAc, pH 5.0, on a Superdex 75 HR column. The proteolytic activity of collected fractions against the PQM substrate (red dashed line; DABCYL-PFFENEQARKDDKN-Glu(EDANS)-NH2) and the iPQM substrate (green dashed line; DABCYL-FYPSQRSETD-Glu(EDANS)-NH2) is given in percentage of degraded substrate. B, cation exchange chromatography of size exclusion chromatography peak 2 on a MiniS PE column equilibrated with 50 mm NH4OAc, pH 5.0. C, subsequent RP-HPLC separation of cation exchange chromatography peak 5 on a <t>Nucleosil</t> 300–5, C4 column equilibrated with 0.05% (v/v) TFA in water. D, SDS-PAGE (8–25%) of C. salei venom and pooled active fractions of each purification step. Bands referred to in the text are lettered.
Guard Column Ec 4 3 Nucleosil 120 3 C8, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c8+column/EC+HPLC+guard+column+(analytical)%2C+NUCLEOSIL+120-3+C8/pmc11684660-188-21-28
Average 93 stars, based on 1 article reviews
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93
MACHEREY NAGEL c8 column
Purification of the native protease. A, size exclusion chromatography of 100 μl of C. salei venom in 100 mm NH4OAc, pH 5.0, on a Superdex 75 HR column. The proteolytic activity of collected fractions against the PQM substrate (red dashed line; DABCYL-PFFENEQARKDDKN-Glu(EDANS)-NH2) and the iPQM substrate (green dashed line; DABCYL-FYPSQRSETD-Glu(EDANS)-NH2) is given in percentage of degraded substrate. B, cation exchange chromatography of size exclusion chromatography peak 2 on a MiniS PE column equilibrated with 50 mm NH4OAc, pH 5.0. C, subsequent RP-HPLC separation of cation exchange chromatography peak 5 on a <t>Nucleosil</t> 300–5, C4 column equilibrated with 0.05% (v/v) TFA in water. D, SDS-PAGE (8–25%) of C. salei venom and pooled active fractions of each purification step. Bands referred to in the text are lettered.
C8 Column, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/c8+column/EC+HPLC+column+(analytical)%2C+NUCLEOSIL+100-7+C8/bio_rxiv__2025__08__22__671756-151-22-30
Average 93 stars, based on 1 article reviews
c8 column - by Bioz Stars, 2026-10
93/100 stars
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90
MACHEREY NAGEL nucleodur c8 ec column
Purification of the native protease. A, size exclusion chromatography of 100 μl of C. salei venom in 100 mm NH4OAc, pH 5.0, on a Superdex 75 HR column. The proteolytic activity of collected fractions against the PQM substrate (red dashed line; DABCYL-PFFENEQARKDDKN-Glu(EDANS)-NH2) and the iPQM substrate (green dashed line; DABCYL-FYPSQRSETD-Glu(EDANS)-NH2) is given in percentage of degraded substrate. B, cation exchange chromatography of size exclusion chromatography peak 2 on a MiniS PE column equilibrated with 50 mm NH4OAc, pH 5.0. C, subsequent RP-HPLC separation of cation exchange chromatography peak 5 on a <t>Nucleosil</t> 300–5, C4 column equilibrated with 0.05% (v/v) TFA in water. D, SDS-PAGE (8–25%) of C. salei venom and pooled active fractions of each purification step. Bands referred to in the text are lettered.
Nucleodur C8 Ec Column, supplied by MACHEREY NAGEL, 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/product/c8+column/VP+HPLC+column+(preparative)%2C+NUCLEODUR+C8+ec/pmc05548851-62-14-24
Average 90 stars, based on 1 article reviews
nucleodur c8 ec column - by Bioz Stars, 2026-10
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Image Search Results


Purification of the native protease. A, size exclusion chromatography of 100 μl of C. salei venom in 100 mm NH4OAc, pH 5.0, on a Superdex 75 HR column. The proteolytic activity of collected fractions against the PQM substrate (red dashed line; DABCYL-PFFENEQARKDDKN-Glu(EDANS)-NH2) and the iPQM substrate (green dashed line; DABCYL-FYPSQRSETD-Glu(EDANS)-NH2) is given in percentage of degraded substrate. B, cation exchange chromatography of size exclusion chromatography peak 2 on a MiniS PE column equilibrated with 50 mm NH4OAc, pH 5.0. C, subsequent RP-HPLC separation of cation exchange chromatography peak 5 on a Nucleosil 300–5, C4 column equilibrated with 0.05% (v/v) TFA in water. D, SDS-PAGE (8–25%) of C. salei venom and pooled active fractions of each purification step. Bands referred to in the text are lettered.

Journal: The Journal of Biological Chemistry

Article Title: Identification of a precursor processing protease from the spider Cupiennius salei essential for venom neurotoxin maturation

doi: 10.1074/jbc.M117.810911

Figure Lengend Snippet: Purification of the native protease. A, size exclusion chromatography of 100 μl of C. salei venom in 100 mm NH4OAc, pH 5.0, on a Superdex 75 HR column. The proteolytic activity of collected fractions against the PQM substrate (red dashed line; DABCYL-PFFENEQARKDDKN-Glu(EDANS)-NH2) and the iPQM substrate (green dashed line; DABCYL-FYPSQRSETD-Glu(EDANS)-NH2) is given in percentage of degraded substrate. B, cation exchange chromatography of size exclusion chromatography peak 2 on a MiniS PE column equilibrated with 50 mm NH4OAc, pH 5.0. C, subsequent RP-HPLC separation of cation exchange chromatography peak 5 on a Nucleosil 300–5, C4 column equilibrated with 0.05% (v/v) TFA in water. D, SDS-PAGE (8–25%) of C. salei venom and pooled active fractions of each purification step. Bands referred to in the text are lettered.

Article Snippet: Third, the eluted proteolytic active fraction was further separated by RP-HPLC on a Nucleosil 300–5, C4 (5 μm, 4.6 × 250 mm, Macherey-Nagel, Düren, Germany) column equilibrated with 0.05% (v/v) TFA in water.

Techniques: Purification, Size-exclusion Chromatography, Activity Assay, Chromatography, SDS Page