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  • 91
    GE Healthcare hiload superdex 75 column
    15% SDS–PAGE analysis of SMU.1108c protein purified by size-exclusion chromatography on a <t>HiLoad</t> <t>Superdex</t> 75 column (column volume 120 ml; GE Healthcare). Lane M , molecular-weight markers (kDa). Lanes 1 and 2, fractions of the target protein
    Hiload Superdex 75 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 91/100, based on 496 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hiload superdex 75 column/product/GE Healthcare
    Average 91 stars, based on 496 article reviews
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    93
    GE Healthcare 16⁄60 hiload superdex 75 column
    15% SDS–PAGE analysis of SMU.1108c protein purified by size-exclusion chromatography on a <t>HiLoad</t> <t>Superdex</t> 75 column (column volume 120 ml; GE Healthcare). Lane M , molecular-weight markers (kDa). Lanes 1 and 2, fractions of the target protein
    16⁄60 Hiload Superdex 75 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/16⁄60 hiload superdex 75 column/product/GE Healthcare
    Average 93 stars, based on 45 article reviews
    Price from $9.99 to $1999.99
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    91
    GE Healthcare hiload 10 300 superdex 75 column
    15% SDS–PAGE analysis of SMU.1108c protein purified by size-exclusion chromatography on a <t>HiLoad</t> <t>Superdex</t> 75 column (column volume 120 ml; GE Healthcare). Lane M , molecular-weight markers (kDa). Lanes 1 and 2, fractions of the target protein
    Hiload 10 300 Superdex 75 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 91/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hiload 10 300 superdex 75 column/product/GE Healthcare
    Average 91 stars, based on 26 article reviews
    Price from $9.99 to $1999.99
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    92
    GE Healthcare hiload 16 60 superdex 75 column
    Purification of recombinant 6xHis-tagged hTLK1B from E. coli . (A) Schematic overview of the purification process using Ni-NTA IMAC and size exclusion chromatography (SEC). (B) SDS-PAGE (12% Tris-Glycine gel) analysis of recombinant hTLK1B through different purification steps. M, molecular weight marker in kDa; lane 1, uninduced soluble fraction after cell homogenization (control); lane 2, IPTG induced soluble fraction (total cell lysate); lane 3, unbound protein fraction; lane 4-6, after-binding column wash fractions; lane 8, eluted hTLK1B after 200 mM imidazole wash. Arrow indicates the position of recombinant 6xHis-tagged hTLK1B protein (64.9 kDa). (C) Chromatogram of HiLoad 16/60 <t>Superdex</t> 75 size-exclusion column after Ni-NTA IMAC step. (D) Immunoblot showing the purified recombinant 6xHis-tagged hTLK1B protein after SEC. His-Tag (D3I10) XP ® Rabbit Monoclonal Antibody (Cat. 12698) was used as a primary antibody. The protein was detected by using Anti-Rabbit IgG Horseradish Peroxidase-linked Secondary Antibody (Cat. 7074) and ECL as a luminescent substrate. The blot image has been cropped for clarity and conciseness. The full-length image of the blots (with multiple exposures) have been included in the Supplementary Figure, S 5 .
    Hiload 16 60 Superdex 75 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 2258 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    GE Healthcare hiload 16 600 superdex 75 columns
    Purification of recombinant 6xHis-tagged hTLK1B from E. coli . (A) Schematic overview of the purification process using Ni-NTA IMAC and size exclusion chromatography (SEC). (B) SDS-PAGE (12% Tris-Glycine gel) analysis of recombinant hTLK1B through different purification steps. M, molecular weight marker in kDa; lane 1, uninduced soluble fraction after cell homogenization (control); lane 2, IPTG induced soluble fraction (total cell lysate); lane 3, unbound protein fraction; lane 4-6, after-binding column wash fractions; lane 8, eluted hTLK1B after 200 mM imidazole wash. Arrow indicates the position of recombinant 6xHis-tagged hTLK1B protein (64.9 kDa). (C) Chromatogram of HiLoad 16/60 <t>Superdex</t> 75 size-exclusion column after Ni-NTA IMAC step. (D) Immunoblot showing the purified recombinant 6xHis-tagged hTLK1B protein after SEC. His-Tag (D3I10) XP ® Rabbit Monoclonal Antibody (Cat. 12698) was used as a primary antibody. The protein was detected by using Anti-Rabbit IgG Horseradish Peroxidase-linked Secondary Antibody (Cat. 7074) and ECL as a luminescent substrate. The blot image has been cropped for clarity and conciseness. The full-length image of the blots (with multiple exposures) have been included in the Supplementary Figure, S 5 .
    Hiload 16 600 Superdex 75 Columns, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hiload 16 600 superdex 75 columns/product/GE Healthcare
    Average 93 stars, based on 45 article reviews
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    88
    GE Healthcare hiload superdex 75 26 60 column
    Purification of protein and nucleic acid components. Elution profiles obtained on a <t>HiLoad</t> Superdex 75 26/60 column, with each species labeled.
    Hiload Superdex 75 26 60 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 202 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 88 stars, based on 202 article reviews
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    hiload superdex 75 26 60 column - by Bioz Stars, 2020-08
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    89
    GE Healthcare hiload 26 600 superdex 75 column
    Purification of protein and nucleic acid components. Elution profiles obtained on a <t>HiLoad</t> Superdex 75 26/60 column, with each species labeled.
    Hiload 26 600 Superdex 75 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 89/100, based on 177 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hiload 26 600 superdex 75 column/product/GE Healthcare
    Average 89 stars, based on 177 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    15% SDS–PAGE analysis of SMU.1108c protein purified by size-exclusion chromatography on a HiLoad Superdex 75 column (column volume 120 ml; GE Healthcare). Lane M , molecular-weight markers (kDa). Lanes 1 and 2, fractions of the target protein

    Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

    Article Title: Purification, crystallization and preliminary crystallographic analysis of SMU.1108c protein from Streptococcus mutans

    doi: 10.1107/S174430911004457X

    Figure Lengend Snippet: 15% SDS–PAGE analysis of SMU.1108c protein purified by size-exclusion chromatography on a HiLoad Superdex 75 column (column volume 120 ml; GE Healthcare). Lane M , molecular-weight markers (kDa). Lanes 1 and 2, fractions of the target protein

    Article Snippet: Further purification was carried out by size-exclusion chromatography on a HiLoad Superdex 75 column (column volume 120 ml; GE Healthcare) using buffer C (20 m M Tris–HCl pH 7.5, 200 m M NaCl).

    Techniques: SDS Page, Purification, Size-exclusion Chromatography, Molecular Weight

    Gel filtration analysis of SARS-CoV 3CL pro S139A mutant. 2 mg/ml of the protein at neutral pH (7.5) was eluted on a HiLoad ™ Superdex ™ 75 prep grade column (GE Healthcare) at a flow rate of 1 ml/min. Marked on the x -axis are the molecular weight (MW) of the four marker proteins (namely ribonuclease A (15.6 kDa), chymotrypsinogen A (22.8 kDa), ovalbumin (48.9 kDa) and albumin (65.4 kDa)) at their specific retention volumes ( Chen et al., 2005 ). The molecular weight of monomeric 3CL pro is about 34 kDa. For S139A mutant, peak A and peak C represent stable dimer and monomer respectively, while peak B represents the equilibrium of monomer and dimer. Peak E and peak D represent wild-type and F140A mutant proteins respectively, which were both in the equilibrium of monomer and dimer. The contents of these peaks were all confirmed by SDS-PAGE (inset) to be SARS-CoV 3CL pro .

    Journal: Virology

    Article Title: Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure

    doi: 10.1016/j.virol.2009.03.034

    Figure Lengend Snippet: Gel filtration analysis of SARS-CoV 3CL pro S139A mutant. 2 mg/ml of the protein at neutral pH (7.5) was eluted on a HiLoad ™ Superdex ™ 75 prep grade column (GE Healthcare) at a flow rate of 1 ml/min. Marked on the x -axis are the molecular weight (MW) of the four marker proteins (namely ribonuclease A (15.6 kDa), chymotrypsinogen A (22.8 kDa), ovalbumin (48.9 kDa) and albumin (65.4 kDa)) at their specific retention volumes ( Chen et al., 2005 ). The molecular weight of monomeric 3CL pro is about 34 kDa. For S139A mutant, peak A and peak C represent stable dimer and monomer respectively, while peak B represents the equilibrium of monomer and dimer. Peak E and peak D represent wild-type and F140A mutant proteins respectively, which were both in the equilibrium of monomer and dimer. The contents of these peaks were all confirmed by SDS-PAGE (inset) to be SARS-CoV 3CL pro .

    Article Snippet: The gel filtration analysis of S139A mutant is performed in the same buffer at 2 mg/ml, on a HiLoad™ Superdex™ 75 prep grade column (GE Healthcare) at a flow rate of 1 ml/min.

    Techniques: Filtration, Mutagenesis, Molecular Weight, Marker, SDS Page

    Purification of recombinant 6xHis-tagged hTLK1B from E. coli . (A) Schematic overview of the purification process using Ni-NTA IMAC and size exclusion chromatography (SEC). (B) SDS-PAGE (12% Tris-Glycine gel) analysis of recombinant hTLK1B through different purification steps. M, molecular weight marker in kDa; lane 1, uninduced soluble fraction after cell homogenization (control); lane 2, IPTG induced soluble fraction (total cell lysate); lane 3, unbound protein fraction; lane 4-6, after-binding column wash fractions; lane 8, eluted hTLK1B after 200 mM imidazole wash. Arrow indicates the position of recombinant 6xHis-tagged hTLK1B protein (64.9 kDa). (C) Chromatogram of HiLoad 16/60 Superdex 75 size-exclusion column after Ni-NTA IMAC step. (D) Immunoblot showing the purified recombinant 6xHis-tagged hTLK1B protein after SEC. His-Tag (D3I10) XP ® Rabbit Monoclonal Antibody (Cat. 12698) was used as a primary antibody. The protein was detected by using Anti-Rabbit IgG Horseradish Peroxidase-linked Secondary Antibody (Cat. 7074) and ECL as a luminescent substrate. The blot image has been cropped for clarity and conciseness. The full-length image of the blots (with multiple exposures) have been included in the Supplementary Figure, S 5 .

    Journal: Scientific Reports

    Article Title: High yield bacterial expression, purification and characterisation of bioactive Human Tousled-like Kinase 1B involved in cancer

    doi: 10.1038/s41598-018-22744-5

    Figure Lengend Snippet: Purification of recombinant 6xHis-tagged hTLK1B from E. coli . (A) Schematic overview of the purification process using Ni-NTA IMAC and size exclusion chromatography (SEC). (B) SDS-PAGE (12% Tris-Glycine gel) analysis of recombinant hTLK1B through different purification steps. M, molecular weight marker in kDa; lane 1, uninduced soluble fraction after cell homogenization (control); lane 2, IPTG induced soluble fraction (total cell lysate); lane 3, unbound protein fraction; lane 4-6, after-binding column wash fractions; lane 8, eluted hTLK1B after 200 mM imidazole wash. Arrow indicates the position of recombinant 6xHis-tagged hTLK1B protein (64.9 kDa). (C) Chromatogram of HiLoad 16/60 Superdex 75 size-exclusion column after Ni-NTA IMAC step. (D) Immunoblot showing the purified recombinant 6xHis-tagged hTLK1B protein after SEC. His-Tag (D3I10) XP ® Rabbit Monoclonal Antibody (Cat. 12698) was used as a primary antibody. The protein was detected by using Anti-Rabbit IgG Horseradish Peroxidase-linked Secondary Antibody (Cat. 7074) and ECL as a luminescent substrate. The blot image has been cropped for clarity and conciseness. The full-length image of the blots (with multiple exposures) have been included in the Supplementary Figure, S 5 .

    Article Snippet: The concentrated protein sample was then further purified and buffer-exchanged into 50 mM Tris-Cl (pH-6.5), 50 mM NaCl and 0.2 mM TCEP by size-exclusion chromatography (SEC) on a HiLoad 16/60 Superdex 75 column (GE Healthcare, Chicago, Illinois, USA).

    Techniques: Purification, Recombinant, Size-exclusion Chromatography, SDS Page, Molecular Weight, Marker, Homogenization, Binding Assay

    Elution profiles of purification of the complex of CCM3 and the MST4 C-terminal domain using a Superdex 75 HiLoad 16/60 column (GE Healthcare). Peak 1 corresponds to the complex of CCM3 (25 kDa) and the MST4 C-terminal domain (8 kDa);

    Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

    Article Title: Crystallization and preliminary crystallographic studies of CCM3 in complex with the C-terminal domain of MST4

    doi: 10.1107/S1744309112016843

    Figure Lengend Snippet: Elution profiles of purification of the complex of CCM3 and the MST4 C-terminal domain using a Superdex 75 HiLoad 16/60 column (GE Healthcare). Peak 1 corresponds to the complex of CCM3 (25 kDa) and the MST4 C-terminal domain (8 kDa);

    Article Snippet: The thioredoxin and six-histidine tag was cleaved from the MST4 C-terminal domain with PreScission protease for 10 h. The sample was then diluted with 15 ml lysis buffer and purified on an Ni–NTA column (Novagen) using the same approach as described above; the eluate was again concentrated to 1 ml by ultrafiltration (Millipore) at 277 K. The sample was then loaded onto a Superdex 75 HiLoad 16/60 column (GE Healthcare) previously equilibrated with 25 m M HEPES pH 7.5, 150 m M sodium chloride, 2 m M DTT.

    Techniques: Purification

    ( a ) Purification of Tc CISSAn by gel-filtration chromatography on a Superdex 75 16/60 HiLoad column. Standards for gel-filtration chromatography (plotted against the secondary axis, dotted curve): peak I, ovalbumin (43 kDa); peak II, carbonic anhydrase (29 kDa); peak III, ribonuclease A (13.7 kDa). Tc CISSA (solid blue curve) eluted as a monomer. Inset: SDS–PAGE analysis of a representative fraction showing migration at the expected molecular mass of 26 kDa and residual thioredoxin tag. Lane MW contains molecular-mass markers (labelled in kDa). ( b ) Further purification of Tc CISSAn by cation-exchange chromatography on a 5 ml HiTrap SP FF column. Inset: SDS–PAGE analysis of a representative fraction showing refined sample free of residual thioredoxin tag.

    Journal: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

    Article Title: Purification, crystallization and X-ray diffraction analysis of Trypanosoma congolense insect-stage surface antigen (TcCISSA)

    doi: 10.1107/S1744309112042686

    Figure Lengend Snippet: ( a ) Purification of Tc CISSAn by gel-filtration chromatography on a Superdex 75 16/60 HiLoad column. Standards for gel-filtration chromatography (plotted against the secondary axis, dotted curve): peak I, ovalbumin (43 kDa); peak II, carbonic anhydrase (29 kDa); peak III, ribonuclease A (13.7 kDa). Tc CISSA (solid blue curve) eluted as a monomer. Inset: SDS–PAGE analysis of a representative fraction showing migration at the expected molecular mass of 26 kDa and residual thioredoxin tag. Lane MW contains molecular-mass markers (labelled in kDa). ( b ) Further purification of Tc CISSAn by cation-exchange chromatography on a 5 ml HiTrap SP FF column. Inset: SDS–PAGE analysis of a representative fraction showing refined sample free of residual thioredoxin tag.

    Article Snippet: The thioredoxin and hexahistidine tags were removed by thrombin cleavage overnight at 291 K in Tris-buffered saline (TBS; 10 m M Tris pH 7.5, 150 m M NaCl) with 2.25 m M calcium chloride and the sample was purified by gel-filtration chromatography on a Superdex 75 16/60 HiLoad column (GE Healthcare) in TBS.

    Techniques: Purification, Filtration, Chromatography, SDS Page, Migration

    Purification of protein and nucleic acid components. Elution profiles obtained on a HiLoad Superdex 75 26/60 column, with each species labeled.

    Journal: PLoS ONE

    Article Title: Biophysical Characterization of G-Quadruplex Recognition in the PITX1 mRNA by the Specificity Domain of the Helicase RHAU

    doi: 10.1371/journal.pone.0144510

    Figure Lengend Snippet: Purification of protein and nucleic acid components. Elution profiles obtained on a HiLoad Superdex 75 26/60 column, with each species labeled.

    Article Snippet: Q2RNA elutes as a compact dominant peak with a shoulder corresponding to larger hydrodynamic volumes ( ) from the HiLoad Superdex 75 26/60 column.

    Techniques: Purification, Labeling

    Purification and processivity of Dpo4-like proteins. ( A ) Scheme for the purification of Dpo4-like proteins. Whole-cell extracts (WC) were clarified and then heat treated at 70°C for 10 min. Denatured E.coli proteins were removed from the extracts by centrifugation (70). Subsequently, the soluble extracts were passed over a Hydroxyapatite Bio-Gel HTP Gel column (HAP) and then a SP Sepharose HP column (Sph). The Saz and Soh Dpo4-like proteins were purified over one additional column, a HiLoad 26/60 Superdex 75 column (data not shown). M designates the Benchmark prestained protein size marker (Invitrogen). ( B ) M13mp18 primer extension reactions using the previously identified S.solfataricus Dpo4 (Sso) and the five newly identified polymerases; S.tengchongensis (Ste), S.shibatae (Ssh), A.infernus (Ain), S.azoricus (Saz) and S.ohwakuensis (Soh). Primer extension of primer M13HTP (5′-CCT TAG AAT CCT TGA AAA CAT AGC GA-3′) annealed to M13mp18 from base pairs 4101 to 4126 was performed at 60°C for 5 min utilizing 10 nM of the M13HTP/M13mp18 primer-template and increasing concentrations of the Dpo4-like enzymes; from left to right 0.2, 2.0 and 20 nM. Replication products were separated on 12%/8 M urea polyacrylamide gels and visualized by PhosphorImager analysis. Primer location and number of nucleotides added are indicated to the left of the gel. ( C ) M13mp18 primer extension reactions using the ‘little finger’ domain chimeric polymerases; A.infernus / S.solfataricus (Ain/Sso) and A.infernus / S.tengchongensis (Ain/Ste).

    Journal: Nucleic Acids Research

    Article Title: Novel thermostable Y-family polymerases: applications for the PCR amplification of damaged or ancient DNAs

    doi: 10.1093/nar/gkj512

    Figure Lengend Snippet: Purification and processivity of Dpo4-like proteins. ( A ) Scheme for the purification of Dpo4-like proteins. Whole-cell extracts (WC) were clarified and then heat treated at 70°C for 10 min. Denatured E.coli proteins were removed from the extracts by centrifugation (70). Subsequently, the soluble extracts were passed over a Hydroxyapatite Bio-Gel HTP Gel column (HAP) and then a SP Sepharose HP column (Sph). The Saz and Soh Dpo4-like proteins were purified over one additional column, a HiLoad 26/60 Superdex 75 column (data not shown). M designates the Benchmark prestained protein size marker (Invitrogen). ( B ) M13mp18 primer extension reactions using the previously identified S.solfataricus Dpo4 (Sso) and the five newly identified polymerases; S.tengchongensis (Ste), S.shibatae (Ssh), A.infernus (Ain), S.azoricus (Saz) and S.ohwakuensis (Soh). Primer extension of primer M13HTP (5′-CCT TAG AAT CCT TGA AAA CAT AGC GA-3′) annealed to M13mp18 from base pairs 4101 to 4126 was performed at 60°C for 5 min utilizing 10 nM of the M13HTP/M13mp18 primer-template and increasing concentrations of the Dpo4-like enzymes; from left to right 0.2, 2.0 and 20 nM. Replication products were separated on 12%/8 M urea polyacrylamide gels and visualized by PhosphorImager analysis. Primer location and number of nucleotides added are indicated to the left of the gel. ( C ) M13mp18 primer extension reactions using the ‘little finger’ domain chimeric polymerases; A.infernus / S.solfataricus (Ain/Sso) and A.infernus / S.tengchongensis (Ain/Ste).

    Article Snippet: The Saz and Soh Dpo4-like proteins were applied to one additional column; a HiLoad 26/60 Superdex 75 column (Amersham Pharmacia Biotech), washed with 100 mM NaCl, 20 mM Tris, pH 7.5, 0.1 mM EDTA and 1 mM DTT to ensure the purity of these two samples.

    Techniques: Purification, Centrifugation, Marker