xk-26 column Ge Healthcare Search Results


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  • 99
    Millipore amicon ultra 15 centrifugal filter
    Amicon Ultra 15 Centrifugal Filter, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 7966 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare xk26 column
    Xk26 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 95/100, based on 183 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare ht sp ion exchange sepharose column
    Ht Sp Ion Exchange Sepharose Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare xk 26 70 column
    Xk 26 70 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 90 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare hiprep 26 10 desalting column
    Hiprep 26 10 Desalting Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 3372 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare sephadex g 25
    Absorption spectra (A) and circular dichroism (CD) spectra of refolded CoxD kept in the absence (B) or presence of ATP-γ-S (C). Solubilized CoxD (5.5 mg ml −1 ) was refolded by rapid dilution (50-fold) in ice cold aqueous Tris (20 mM) under magnetic stirring. The solution was immediately adjusted to pH 9.0 (A, dashed line) and subsequently brought to pH 8.0 (A, dotted line) in pH increments of 0.2 per 24 h as specified in   Materials and Methods . Then the protein was concentrated to 1.04 mg ml −1  by ultra-filtration (A, solid line). The CD spectra of CoxD (0.471 mg ml −1 ; 10 mM KH 2 PO 4 /KOH, pH 8.0) are shown in (B). The CD spectra of CoxD (0.537 mg ml −1 ; 10 mM KH 2 PO 4 /KOH, pH 8.0) in the presence of 0.1 mM MgATP-γ-S are shown in (C). After 2 h of incubation with MgATP-γ-S, excess nucleotides were removed by gel filtration on Sephadex G-25. All data were recorded at 20°C. Raw data are shown in black. The smoothed data used for secondary structure estimation and the back-calculated CD-spectrum based on deconvolution with the CDSSTR algorithm   [21]  is depicted in red and blue, respectively. For further details refer to   Materials and Methods .
    Sephadex G 25, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 1606 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare size exclusion chromatography
    Proportion of dimers present as a function of time for 56.3 μM (assuming all proteins are monomers) freshly prepared AFABP samples that were stored in buffers saturated with oxygen (blue curve) or infused with oxygen-scrubbed nitrogen gas (red curve). Percentages were derived from elution profiles of <t>Superdex</t> 75 size exclusion gel filtration chromatography analogous to those illustrated in Fig. 3 . Error bars denote results from triplicate GF runs on the same sample. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article).
    Size Exclusion Chromatography, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 33382 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Qiagen ni nta agarose
    Proportion of dimers present as a function of time for 56.3 μM (assuming all proteins are monomers) freshly prepared AFABP samples that were stored in buffers saturated with oxygen (blue curve) or infused with oxygen-scrubbed nitrogen gas (red curve). Percentages were derived from elution profiles of <t>Superdex</t> 75 size exclusion gel filtration chromatography analogous to those illustrated in Fig. 3 . Error bars denote results from triplicate GF runs on the same sample. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article).
    Ni Nta Agarose, supplied by Qiagen, used in various techniques. Bioz Stars score: 99/100, based on 30007 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare histrap ff crude column
    Proportion of dimers present as a function of time for 56.3 μM (assuming all proteins are monomers) freshly prepared AFABP samples that were stored in buffers saturated with oxygen (blue curve) or infused with oxygen-scrubbed nitrogen gas (red curve). Percentages were derived from elution profiles of <t>Superdex</t> 75 size exclusion gel filtration chromatography analogous to those illustrated in Fig. 3 . Error bars denote results from triplicate GF runs on the same sample. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article).
    Histrap Ff Crude Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 2164 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore amicon ultra
    Proportion of dimers present as a function of time for 56.3 μM (assuming all proteins are monomers) freshly prepared AFABP samples that were stored in buffers saturated with oxygen (blue curve) or infused with oxygen-scrubbed nitrogen gas (red curve). Percentages were derived from elution profiles of <t>Superdex</t> 75 size exclusion gel filtration chromatography analogous to those illustrated in Fig. 3 . Error bars denote results from triplicate GF runs on the same sample. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article).
    Amicon Ultra, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 8952 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare sephadex g 50 column
    Proportion of dimers present as a function of time for 56.3 μM (assuming all proteins are monomers) freshly prepared AFABP samples that were stored in buffers saturated with oxygen (blue curve) or infused with oxygen-scrubbed nitrogen gas (red curve). Percentages were derived from elution profiles of <t>Superdex</t> 75 size exclusion gel filtration chromatography analogous to those illustrated in Fig. 3 . Error bars denote results from triplicate GF runs on the same sample. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article).
    Sephadex G 50 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 98/100, based on 685 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare glutathione sepharose 4b
    Phosphorylation of SV2A at Cluster-2 promotes the interaction with synaptotagmin-1. Biotinylated dephosphorylated or triply phosphorylated (Ser80, Ser81, and Thr84) peptides that encompassed the Cluster-2 region of SV2A were conjugated to <t>streptavidin–Sepharose</t>
    Glutathione Sepharose 4b, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 23914 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare hisprep imac column
    Phosphorylation of SV2A at Cluster-2 promotes the interaction with synaptotagmin-1. Biotinylated dephosphorylated or triply phosphorylated (Ser80, Ser81, and Thr84) peptides that encompassed the Cluster-2 region of SV2A were conjugated to <t>streptavidin–Sepharose</t>
    Hisprep Imac Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare histrap hp
    Phosphorylation of SV2A at Cluster-2 promotes the interaction with synaptotagmin-1. Biotinylated dephosphorylated or triply phosphorylated (Ser80, Ser81, and Thr84) peptides that encompassed the Cluster-2 region of SV2A were conjugated to <t>streptavidin–Sepharose</t>
    Histrap Hp, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 5241 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Research Products International m maltose
    Phosphorylation of SV2A at Cluster-2 promotes the interaction with synaptotagmin-1. Biotinylated dephosphorylated or triply phosphorylated (Ser80, Ser81, and Thr84) peptides that encompassed the Cluster-2 region of SV2A were conjugated to <t>streptavidin–Sepharose</t>
    M Maltose, supplied by Research Products International, used in various techniques. Bioz Stars score: 88/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare ni sepharose 6 ff
    Phosphorylation of SV2A at Cluster-2 promotes the interaction with synaptotagmin-1. Biotinylated dephosphorylated or triply phosphorylated (Ser80, Ser81, and Thr84) peptides that encompassed the Cluster-2 region of SV2A were conjugated to <t>streptavidin–Sepharose</t>
    Ni Sepharose 6 Ff, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare q sepharose fast flow column
    Partial purification of AcoA from S. coelicolor crude extracts. S. coelicolor crude extract (lane 1) was fractionated by <t>Q-Sepharose</t> anion-exchange chromatography (lane 2), Source Q anion-exchange chromatography (lane 3), Source S cation-exchange chromatography (lane 4), and Superose 6 gel filtration chromatography (lane 5). Representative samples from each chromatographic step were resolved by SDS-PAGE and stained with Coomassie brilliant blue. The molecular masses of the protein marker present in lane M are indicated on the right (in kilodaltons). The arrow on the right designates the position of AcoA.
    Q Sepharose Fast Flow Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 1412 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex 75 column
    Purification of MTC28-BAP protein. Chromatogram showing (A) Elution profile of H10-T-MTC28-BAP protein on Ni Sepharose Fast Flow (NiFF) affinity column. Fraction numbers 6–17 were pooled (NiFF pool). (B) Elution profile of H10-T-MTC28-BAP protein on <t>Superdex</t> 75 gel-filtration column. Fraction numbers 16–24 were pooled (GFC pool). The GFC pool was treated with H6-TEV protease to cleave H10 tag from the protein followed by removal of cleaved tag and H6-TEV protease using Ni-affinity chromatography. (C) Elution profile of MTC28-BAP protein on Q Sepharose HP column. Fraction numbers 22–27 were pooled (QHP pool). (D) SDS-PAGE analysis of H10-T-MTC28-BAP protein at different stages during purification. The samples were analyzed by 0.1% SDS-12.5% PAGE under reducing conditions. The protein bands were visualized with Coomassie brilliant blue R-250 staining. Lane M, molecular weight marker, broad range (Bio-Rad, Hercules, CA) (shown in kDa); Lane 1, total cell after homogenization; Lane 2, High-High Speed Supernatant; Lane 3, NiFF pool; Lane 4, GFC pool; Lane 5, NiFF-TT pool (after desalting); Lane 6, QHP pool.
    Superdex 75 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 9348 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare superdex
    Purification of Arp2/3 complex using <t>Superdex</t> 200pg gel filtration chromatography
    Superdex, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 33662 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare xk 26 100 column
    Purification of Arp2/3 complex using <t>Superdex</t> 200pg gel filtration chromatography
    Xk 26 100 Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 105 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare 16 20 xk column
    Purification of Arp2/3 complex using <t>Superdex</t> 200pg gel filtration chromatography
    16 20 Xk Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Absorption spectra (A) and circular dichroism (CD) spectra of refolded CoxD kept in the absence (B) or presence of ATP-γ-S (C). Solubilized CoxD (5.5 mg ml −1 ) was refolded by rapid dilution (50-fold) in ice cold aqueous Tris (20 mM) under magnetic stirring. The solution was immediately adjusted to pH 9.0 (A, dashed line) and subsequently brought to pH 8.0 (A, dotted line) in pH increments of 0.2 per 24 h as specified in   Materials and Methods . Then the protein was concentrated to 1.04 mg ml −1  by ultra-filtration (A, solid line). The CD spectra of CoxD (0.471 mg ml −1 ; 10 mM KH 2 PO 4 /KOH, pH 8.0) are shown in (B). The CD spectra of CoxD (0.537 mg ml −1 ; 10 mM KH 2 PO 4 /KOH, pH 8.0) in the presence of 0.1 mM MgATP-γ-S are shown in (C). After 2 h of incubation with MgATP-γ-S, excess nucleotides were removed by gel filtration on Sephadex G-25. All data were recorded at 20°C. Raw data are shown in black. The smoothed data used for secondary structure estimation and the back-calculated CD-spectrum based on deconvolution with the CDSSTR algorithm   [21]  is depicted in red and blue, respectively. For further details refer to   Materials and Methods .

    Journal: PLoS ONE

    Article Title: The CoxD Protein, a Novel AAA+ ATPase Involved in Metal Cluster Assembly: Hydrolysis of Nucleotide-Triphosphates and Oligomerization

    doi: 10.1371/journal.pone.0047424

    Figure Lengend Snippet: Absorption spectra (A) and circular dichroism (CD) spectra of refolded CoxD kept in the absence (B) or presence of ATP-γ-S (C). Solubilized CoxD (5.5 mg ml −1 ) was refolded by rapid dilution (50-fold) in ice cold aqueous Tris (20 mM) under magnetic stirring. The solution was immediately adjusted to pH 9.0 (A, dashed line) and subsequently brought to pH 8.0 (A, dotted line) in pH increments of 0.2 per 24 h as specified in Materials and Methods . Then the protein was concentrated to 1.04 mg ml −1 by ultra-filtration (A, solid line). The CD spectra of CoxD (0.471 mg ml −1 ; 10 mM KH 2 PO 4 /KOH, pH 8.0) are shown in (B). The CD spectra of CoxD (0.537 mg ml −1 ; 10 mM KH 2 PO 4 /KOH, pH 8.0) in the presence of 0.1 mM MgATP-γ-S are shown in (C). After 2 h of incubation with MgATP-γ-S, excess nucleotides were removed by gel filtration on Sephadex G-25. All data were recorded at 20°C. Raw data are shown in black. The smoothed data used for secondary structure estimation and the back-calculated CD-spectrum based on deconvolution with the CDSSTR algorithm [21] is depicted in red and blue, respectively. For further details refer to Materials and Methods .

    Article Snippet: Where indicated, sucrose was removed from samples by gel filtration on Sephadex G-25 (PD-10 pre-packed columns, GE Healthcare, Little Chalfont, UK).

    Techniques: Filtration, Incubation

    Proportion of dimers present as a function of time for 56.3 μM (assuming all proteins are monomers) freshly prepared AFABP samples that were stored in buffers saturated with oxygen (blue curve) or infused with oxygen-scrubbed nitrogen gas (red curve). Percentages were derived from elution profiles of Superdex 75 size exclusion gel filtration chromatography analogous to those illustrated in Fig. 3 . Error bars denote results from triplicate GF runs on the same sample. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article).

    Journal: Biochemistry and Biophysics Reports

    Article Title: Protocols and pitfalls in obtaining fatty acid-binding proteins for biophysical studies of ligand-protein and protein-protein interactions

    doi: 10.1016/j.bbrep.2017.05.001

    Figure Lengend Snippet: Proportion of dimers present as a function of time for 56.3 μM (assuming all proteins are monomers) freshly prepared AFABP samples that were stored in buffers saturated with oxygen (blue curve) or infused with oxygen-scrubbed nitrogen gas (red curve). Percentages were derived from elution profiles of Superdex 75 size exclusion gel filtration chromatography analogous to those illustrated in Fig. 3 . Error bars denote results from triplicate GF runs on the same sample. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article).

    Article Snippet: 2.3 Isolation and development of apo-AFABP oligomers To verify the oligomerization state of the AFABP protein, a prepacked XK26/40 column of Superdex 75 (GE Healthcare) was used for gel filtration chromatography.

    Techniques: Derivative Assay, Filtration, Chromatography

    Phosphorylation of SV2A at Cluster-2 promotes the interaction with synaptotagmin-1. Biotinylated dephosphorylated or triply phosphorylated (Ser80, Ser81, and Thr84) peptides that encompassed the Cluster-2 region of SV2A were conjugated to streptavidin–Sepharose

    Journal: The Journal of Neuroscience

    Article Title: Phosphorylation of Synaptic Vesicle Protein 2A at Thr84 by Casein Kinase 1 Family Kinases Controls the Specific Retrieval of Synaptotagmin-1

    doi: 10.1523/JNEUROSCI.4248-14.2015

    Figure Lengend Snippet: Phosphorylation of SV2A at Cluster-2 promotes the interaction with synaptotagmin-1. Biotinylated dephosphorylated or triply phosphorylated (Ser80, Ser81, and Thr84) peptides that encompassed the Cluster-2 region of SV2A were conjugated to streptavidin–Sepharose

    Article Snippet: Cells were lysed by freeze–thawing at −80°C, followed by sonication on ice, and the cell extract was cleared from intact cells and debris by centrifugation at 30,000 × g and 4°C for 20 min. GST-tagged protein was purified by affinity chromatography in a 16/20 XK column (GE Healthcare) packed with 10 ml of glutathione Sepharose 4B (GE Healthcare) in 50 m m HEPES, pH 7.5, and 250 m m NaCl, and bound protein was eluted with 40 m m reduced glutathione, 50 m m HEPES, pH 7.5, and 250 m m NaCl.

    Techniques:

    Partial purification of AcoA from S. coelicolor crude extracts. S. coelicolor crude extract (lane 1) was fractionated by Q-Sepharose anion-exchange chromatography (lane 2), Source Q anion-exchange chromatography (lane 3), Source S cation-exchange chromatography (lane 4), and Superose 6 gel filtration chromatography (lane 5). Representative samples from each chromatographic step were resolved by SDS-PAGE and stained with Coomassie brilliant blue. The molecular masses of the protein marker present in lane M are indicated on the right (in kilodaltons). The arrow on the right designates the position of AcoA.

    Journal: Journal of Bacteriology

    Article Title: Roles of Aconitase in Growth, Metabolism, and Morphological Differentiation of Streptomyces coelicolor

    doi: 10.1128/JB.183.10.3193-3203.2001

    Figure Lengend Snippet: Partial purification of AcoA from S. coelicolor crude extracts. S. coelicolor crude extract (lane 1) was fractionated by Q-Sepharose anion-exchange chromatography (lane 2), Source Q anion-exchange chromatography (lane 3), Source S cation-exchange chromatography (lane 4), and Superose 6 gel filtration chromatography (lane 5). Representative samples from each chromatographic step were resolved by SDS-PAGE and stained with Coomassie brilliant blue. The molecular masses of the protein marker present in lane M are indicated on the right (in kilodaltons). The arrow on the right designates the position of AcoA.

    Article Snippet: The supernatant was loaded onto a 50-ml Q-Sepharose Fast Flow column (XK26/20; Amersham Pharmacia) equilibrated in buffer A and eluted with a linear gradient from 0.1 to 1 M NaCl in buffer A.

    Techniques: Purification, Chromatography, Filtration, SDS Page, Staining, Marker

    Purification of MTC28-BAP protein. Chromatogram showing (A) Elution profile of H10-T-MTC28-BAP protein on Ni Sepharose Fast Flow (NiFF) affinity column. Fraction numbers 6–17 were pooled (NiFF pool). (B) Elution profile of H10-T-MTC28-BAP protein on Superdex 75 gel-filtration column. Fraction numbers 16–24 were pooled (GFC pool). The GFC pool was treated with H6-TEV protease to cleave H10 tag from the protein followed by removal of cleaved tag and H6-TEV protease using Ni-affinity chromatography. (C) Elution profile of MTC28-BAP protein on Q Sepharose HP column. Fraction numbers 22–27 were pooled (QHP pool). (D) SDS-PAGE analysis of H10-T-MTC28-BAP protein at different stages during purification. The samples were analyzed by 0.1% SDS-12.5% PAGE under reducing conditions. The protein bands were visualized with Coomassie brilliant blue R-250 staining. Lane M, molecular weight marker, broad range (Bio-Rad, Hercules, CA) (shown in kDa); Lane 1, total cell after homogenization; Lane 2, High-High Speed Supernatant; Lane 3, NiFF pool; Lane 4, GFC pool; Lane 5, NiFF-TT pool (after desalting); Lane 6, QHP pool.

    Journal: PLoS ONE

    Article Title: Biotin-tagged proteins: Reagents for efficient ELISA-based serodiagnosis and phage display-based affinity selection

    doi: 10.1371/journal.pone.0191315

    Figure Lengend Snippet: Purification of MTC28-BAP protein. Chromatogram showing (A) Elution profile of H10-T-MTC28-BAP protein on Ni Sepharose Fast Flow (NiFF) affinity column. Fraction numbers 6–17 were pooled (NiFF pool). (B) Elution profile of H10-T-MTC28-BAP protein on Superdex 75 gel-filtration column. Fraction numbers 16–24 were pooled (GFC pool). The GFC pool was treated with H6-TEV protease to cleave H10 tag from the protein followed by removal of cleaved tag and H6-TEV protease using Ni-affinity chromatography. (C) Elution profile of MTC28-BAP protein on Q Sepharose HP column. Fraction numbers 22–27 were pooled (QHP pool). (D) SDS-PAGE analysis of H10-T-MTC28-BAP protein at different stages during purification. The samples were analyzed by 0.1% SDS-12.5% PAGE under reducing conditions. The protein bands were visualized with Coomassie brilliant blue R-250 staining. Lane M, molecular weight marker, broad range (Bio-Rad, Hercules, CA) (shown in kDa); Lane 1, total cell after homogenization; Lane 2, High-High Speed Supernatant; Lane 3, NiFF pool; Lane 4, GFC pool; Lane 5, NiFF-TT pool (after desalting); Lane 6, QHP pool.

    Article Snippet: For H10-T-MTC28-BAP protein, gel-filtration chromatography of NiFF pool was performed on 480 ml Superdex 75 column (XK 26/100, GE Healthcare).

    Techniques: Purification, Flow Cytometry, Affinity Column, Filtration, Affinity Chromatography, SDS Page, Polyacrylamide Gel Electrophoresis, Staining, Molecular Weight, Marker, Homogenization

    Purification of Arp2/3 complex using Superdex 200pg gel filtration chromatography

    Journal: Methods in molecular biology (Clifton, N.J.)

    Article Title: Purification of Arp2/3 complex from Saccharomyces cerevisiae

    doi: 10.1007/978-1-62703-538-5_15

    Figure Lengend Snippet: Purification of Arp2/3 complex using Superdex 200pg gel filtration chromatography

    Article Snippet: Superdex 200 pg column: This is a prepacked HiLoad 26/600 Superdex 200 pg column, with 320 mL of resin in XK26/600 column hardware (GE# 28-9893-36).

    Techniques: Purification, Filtration, Chromatography

    Further purification of Arp2/3 complex using Superdex 200pg gel filtration chromatography

    Journal: Methods in molecular biology (Clifton, N.J.)

    Article Title: Purification of Arp2/3 complex from Saccharomyces cerevisiae

    doi: 10.1007/978-1-62703-538-5_15

    Figure Lengend Snippet: Further purification of Arp2/3 complex using Superdex 200pg gel filtration chromatography

    Article Snippet: Superdex 200 pg column: This is a prepacked HiLoad 26/600 Superdex 200 pg column, with 320 mL of resin in XK26/600 column hardware (GE# 28-9893-36).

    Techniques: Purification, Filtration, Chromatography