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Bio-Rad m nacl
Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm <t>NaCl,</t> 1 mm <t>DTT,</t> pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.
M Nacl, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "The SCAN Domain of ZNF174 Is a Dimer"

Article Title: The SCAN Domain of ZNF174 Is a Dimer

Journal: The Journal of biological chemistry

doi: 10.1074/jbc.M109815200

Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.
Figure Legend Snippet: Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.

Techniques Used: Sedimentation, Recombinant, Protein Concentration

Purification of recombinant SCAN domain. A , 4 –12% gradient SDS-polyacrylamide gel. Lane 1 , protein standards; lane 2 , supernatant; lane 3 , GST-Sepharose affinity-purified GST-SCAN domain fusion protein before thrombin cleavage; lane 4 , eluate containing SCAN domain after cleavage with thrombin; lane 5 , SCAN domain after cation exchange chromatography; lane 6 , SCAN domain after size exclusion chromatography. B , analytical size exclusion chromatography of the purified SCAN domain. Recombinant purified SCAN domain (225 μm subunit) in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, was applied to an analytical gel filtration column. The column was calibrated under the same conditions with the following protein standards: thyroglobulin, 670,000 Da, 8.9 min; IgG, 158,000 Da, 11.2 min; ovalbumin, 44,000 Da, 12.5 min; myoglobin 17,000 Da, 14.5 min. The indicated positions for monomer, dimer, and trimer were determined from a linear regression of the standards using a subunit molecular mass of 11.56 kDa for the SCAN domain.
Figure Legend Snippet: Purification of recombinant SCAN domain. A , 4 –12% gradient SDS-polyacrylamide gel. Lane 1 , protein standards; lane 2 , supernatant; lane 3 , GST-Sepharose affinity-purified GST-SCAN domain fusion protein before thrombin cleavage; lane 4 , eluate containing SCAN domain after cleavage with thrombin; lane 5 , SCAN domain after cation exchange chromatography; lane 6 , SCAN domain after size exclusion chromatography. B , analytical size exclusion chromatography of the purified SCAN domain. Recombinant purified SCAN domain (225 μm subunit) in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, was applied to an analytical gel filtration column. The column was calibrated under the same conditions with the following protein standards: thyroglobulin, 670,000 Da, 8.9 min; IgG, 158,000 Da, 11.2 min; ovalbumin, 44,000 Da, 12.5 min; myoglobin 17,000 Da, 14.5 min. The indicated positions for monomer, dimer, and trimer were determined from a linear regression of the standards using a subunit molecular mass of 11.56 kDa for the SCAN domain.

Techniques Used: Purification, Recombinant, Affinity Purification, Chromatography, Size-exclusion Chromatography, Filtration

CD spectroscopy of the SCAN domain. CD spectroscopy of the purified SCAN domain was performed in 25 mm phosphate, 200 mm NaCl, 0.2 mm DTT, pH 6.5. A , CD spectrum of the isolated SCAN domain of ZNF174 (25 μm subunit) at 4 °C. B , thermal denaturation of the SCAN domain of ZNF174. The molar ellipticity at 222 nm at increasing temperatures was determined for the SCAN domain at either 5 μm subunit ( closed circles ) or 2 μm subunit ( open circles ).
Figure Legend Snippet: CD spectroscopy of the SCAN domain. CD spectroscopy of the purified SCAN domain was performed in 25 mm phosphate, 200 mm NaCl, 0.2 mm DTT, pH 6.5. A , CD spectrum of the isolated SCAN domain of ZNF174 (25 μm subunit) at 4 °C. B , thermal denaturation of the SCAN domain of ZNF174. The molar ellipticity at 222 nm at increasing temperatures was determined for the SCAN domain at either 5 μm subunit ( closed circles ) or 2 μm subunit ( open circles ).

Techniques Used: Spectroscopy, Purification, Isolation

2) Product Images from "Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster *"

Article Title: Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M115.711218

Dioxygen does not affect cluster transfer, whereas it increases cluster lability. Reactions were performed in 50 m m Bis-Tris, pH 6.2, 100 m m NaCl at 25 °C using oxidized holo-mNT and apo-FDX (20 μ m concentrations of each protein) for cluster
Figure Legend Snippet: Dioxygen does not affect cluster transfer, whereas it increases cluster lability. Reactions were performed in 50 m m Bis-Tris, pH 6.2, 100 m m NaCl at 25 °C using oxidized holo-mNT and apo-FDX (20 μ m concentrations of each protein) for cluster

Techniques Used:

Denaturation of oxidized holo-mNT under anaerobic conditions results in reduction of the remaining holo-mNT. Studies were performed with 250 μ m 15 N-labeled mNT in 50 m m Bis-Tris, pH 6.2, 100 m m NaCl at 298 K. A , mNT denaturation under aerobic
Figure Legend Snippet: Denaturation of oxidized holo-mNT under anaerobic conditions results in reduction of the remaining holo-mNT. Studies were performed with 250 μ m 15 N-labeled mNT in 50 m m Bis-Tris, pH 6.2, 100 m m NaCl at 298 K. A , mNT denaturation under aerobic

Techniques Used: Labeling

Related Articles

Filtration:

Article Title: The SCAN Domain of ZNF174 Is a Dimer
Article Snippet: .. Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad). .. The column was calibrated under the same conditions with the following protein standards (thyroglobulin, molecular weight 670,000; IgG, 158,000; ovalbumin, 44,000; myoglobin, 17,000).

Chromatography:

Article Title: The SCAN Domain of ZNF174 Is a Dimer
Article Snippet: .. Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad). .. The column was calibrated under the same conditions with the following protein standards (thyroglobulin, molecular weight 670,000; IgG, 158,000; ovalbumin, 44,000; myoglobin, 17,000).

Bradford Assay:

Article Title: The Single Subunit Transmembrane E3 Ligase Gene Related to Anergy in Lymphocytes (GRAIL) Captures and Then Ubiquitinates Transmembrane Proteins across the Cell Membrane *
Article Snippet: .. Cells were lysed with Brij96 lysis buffer to detect protein-protein interactions (20 m m Tris-HCl (pH 7.5), 150 m m NaCl, 1% Brij96, protease inhibitors), and protein concentration was measured by Bradford assay (Bio-Rad). .. For ubiquitination assays, cells were incubated with ALLN (10 μg/ml) for 1.5–2 h at 37 °C prior to lysis.

Western Blot:

Article Title: NOX2-dependent ATM kinase activation dictates pro-inflammatory macrophage phenotype and improves effectiveness to radiation therapy
Article Snippet: .. After three washings in NEHN buffer containing 300 m M NaCl and one in NEHN buffer with 600 m M NaCl, immunoprecipitates and protein inputs were boiled in the Laemmli buffer (Bio-Rad, Marnes-la-coquette, France) for 10 min at 95 °C and analyzed by western blot for the indicated antibodies. .. Hydrogen peroxide and anion superoxide production were determined by staining cells with 5 μ M of 2,7-dichlorodihydrofluorescein diacetate (H2 DCFDA, #D6883, Sigma-Aldrich) for 40 min at 37 °C.

Size-exclusion Chromatography:

Article Title: The SCAN Domain of ZNF174 Is a Dimer
Article Snippet: .. Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad). .. The column was calibrated under the same conditions with the following protein standards (thyroglobulin, molecular weight 670,000; IgG, 158,000; ovalbumin, 44,000; myoglobin, 17,000).

Purification:

Article Title: The extreme C-terminal region of kindlin-2 is critical to its regulation of integrin activation
Article Snippet: .. The purified proteins were dialyzed against 50 m m Tris, pH 8.0, containing 150 m m NaCl, quantified using Bio-Rad protein assay kits, and assessed for homogeneity by SDS-PAGE and their elution from the Superdex columns ( ). .. The hexahistidine-tagged human kindlin-2 F2 subdomain (residues 281–569) was bacterially expressed and purified as described previously ( ).

Article Title: The SCAN Domain of ZNF174 Is a Dimer
Article Snippet: .. Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad). .. The column was calibrated under the same conditions with the following protein standards (thyroglobulin, molecular weight 670,000; IgG, 158,000; ovalbumin, 44,000; myoglobin, 17,000).

Protein Concentration:

Article Title: The Single Subunit Transmembrane E3 Ligase Gene Related to Anergy in Lymphocytes (GRAIL) Captures and Then Ubiquitinates Transmembrane Proteins across the Cell Membrane *
Article Snippet: .. Cells were lysed with Brij96 lysis buffer to detect protein-protein interactions (20 m m Tris-HCl (pH 7.5), 150 m m NaCl, 1% Brij96, protease inhibitors), and protein concentration was measured by Bradford assay (Bio-Rad). .. For ubiquitination assays, cells were incubated with ALLN (10 μg/ml) for 1.5–2 h at 37 °C prior to lysis.

Lysis:

Article Title: The Single Subunit Transmembrane E3 Ligase Gene Related to Anergy in Lymphocytes (GRAIL) Captures and Then Ubiquitinates Transmembrane Proteins across the Cell Membrane *
Article Snippet: .. Cells were lysed with Brij96 lysis buffer to detect protein-protein interactions (20 m m Tris-HCl (pH 7.5), 150 m m NaCl, 1% Brij96, protease inhibitors), and protein concentration was measured by Bradford assay (Bio-Rad). .. For ubiquitination assays, cells were incubated with ALLN (10 μg/ml) for 1.5–2 h at 37 °C prior to lysis.

Recombinant:

Article Title: The SCAN Domain of ZNF174 Is a Dimer
Article Snippet: .. Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad). .. The column was calibrated under the same conditions with the following protein standards (thyroglobulin, molecular weight 670,000; IgG, 158,000; ovalbumin, 44,000; myoglobin, 17,000).

SDS Page:

Article Title: The extreme C-terminal region of kindlin-2 is critical to its regulation of integrin activation
Article Snippet: .. The purified proteins were dialyzed against 50 m m Tris, pH 8.0, containing 150 m m NaCl, quantified using Bio-Rad protein assay kits, and assessed for homogeneity by SDS-PAGE and their elution from the Superdex columns ( ). .. The hexahistidine-tagged human kindlin-2 F2 subdomain (residues 281–569) was bacterially expressed and purified as described previously ( ).

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    Bio-Rad m nacl
    Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm <t>NaCl,</t> 1 mm <t>DTT,</t> pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.
    M Nacl, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/m nacl/product/Bio-Rad
    Average 92 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    m nacl - by Bioz Stars, 2021-01
    92/100 stars
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    Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.

    Journal: The Journal of biological chemistry

    Article Title: The SCAN Domain of ZNF174 Is a Dimer

    doi: 10.1074/jbc.M109815200

    Figure Lengend Snippet: Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.

    Article Snippet: Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad).

    Techniques: Sedimentation, Recombinant, Protein Concentration

    Purification of recombinant SCAN domain. A , 4 –12% gradient SDS-polyacrylamide gel. Lane 1 , protein standards; lane 2 , supernatant; lane 3 , GST-Sepharose affinity-purified GST-SCAN domain fusion protein before thrombin cleavage; lane 4 , eluate containing SCAN domain after cleavage with thrombin; lane 5 , SCAN domain after cation exchange chromatography; lane 6 , SCAN domain after size exclusion chromatography. B , analytical size exclusion chromatography of the purified SCAN domain. Recombinant purified SCAN domain (225 μm subunit) in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, was applied to an analytical gel filtration column. The column was calibrated under the same conditions with the following protein standards: thyroglobulin, 670,000 Da, 8.9 min; IgG, 158,000 Da, 11.2 min; ovalbumin, 44,000 Da, 12.5 min; myoglobin 17,000 Da, 14.5 min. The indicated positions for monomer, dimer, and trimer were determined from a linear regression of the standards using a subunit molecular mass of 11.56 kDa for the SCAN domain.

    Journal: The Journal of biological chemistry

    Article Title: The SCAN Domain of ZNF174 Is a Dimer

    doi: 10.1074/jbc.M109815200

    Figure Lengend Snippet: Purification of recombinant SCAN domain. A , 4 –12% gradient SDS-polyacrylamide gel. Lane 1 , protein standards; lane 2 , supernatant; lane 3 , GST-Sepharose affinity-purified GST-SCAN domain fusion protein before thrombin cleavage; lane 4 , eluate containing SCAN domain after cleavage with thrombin; lane 5 , SCAN domain after cation exchange chromatography; lane 6 , SCAN domain after size exclusion chromatography. B , analytical size exclusion chromatography of the purified SCAN domain. Recombinant purified SCAN domain (225 μm subunit) in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, was applied to an analytical gel filtration column. The column was calibrated under the same conditions with the following protein standards: thyroglobulin, 670,000 Da, 8.9 min; IgG, 158,000 Da, 11.2 min; ovalbumin, 44,000 Da, 12.5 min; myoglobin 17,000 Da, 14.5 min. The indicated positions for monomer, dimer, and trimer were determined from a linear regression of the standards using a subunit molecular mass of 11.56 kDa for the SCAN domain.

    Article Snippet: Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad).

    Techniques: Purification, Recombinant, Affinity Purification, Chromatography, Size-exclusion Chromatography, Filtration

    CD spectroscopy of the SCAN domain. CD spectroscopy of the purified SCAN domain was performed in 25 mm phosphate, 200 mm NaCl, 0.2 mm DTT, pH 6.5. A , CD spectrum of the isolated SCAN domain of ZNF174 (25 μm subunit) at 4 °C. B , thermal denaturation of the SCAN domain of ZNF174. The molar ellipticity at 222 nm at increasing temperatures was determined for the SCAN domain at either 5 μm subunit ( closed circles ) or 2 μm subunit ( open circles ).

    Journal: The Journal of biological chemistry

    Article Title: The SCAN Domain of ZNF174 Is a Dimer

    doi: 10.1074/jbc.M109815200

    Figure Lengend Snippet: CD spectroscopy of the SCAN domain. CD spectroscopy of the purified SCAN domain was performed in 25 mm phosphate, 200 mm NaCl, 0.2 mm DTT, pH 6.5. A , CD spectrum of the isolated SCAN domain of ZNF174 (25 μm subunit) at 4 °C. B , thermal denaturation of the SCAN domain of ZNF174. The molar ellipticity at 222 nm at increasing temperatures was determined for the SCAN domain at either 5 μm subunit ( closed circles ) or 2 μm subunit ( open circles ).

    Article Snippet: Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad).

    Techniques: Spectroscopy, Purification, Isolation

    Dioxygen does not affect cluster transfer, whereas it increases cluster lability. Reactions were performed in 50 m m Bis-Tris, pH 6.2, 100 m m NaCl at 25 °C using oxidized holo-mNT and apo-FDX (20 μ m concentrations of each protein) for cluster

    Journal: The Journal of Biological Chemistry

    Article Title: Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster *

    doi: 10.1074/jbc.M115.711218

    Figure Lengend Snippet: Dioxygen does not affect cluster transfer, whereas it increases cluster lability. Reactions were performed in 50 m m Bis-Tris, pH 6.2, 100 m m NaCl at 25 °C using oxidized holo-mNT and apo-FDX (20 μ m concentrations of each protein) for cluster

    Article Snippet: When specified, DTT was removed, and buffer was exchanged with 50 m m Bis-Tris, pH 6.2, 100 m m NaCl using a Micro Bio-Spin Size Exclusion column (Bio-Rad).

    Techniques:

    Denaturation of oxidized holo-mNT under anaerobic conditions results in reduction of the remaining holo-mNT. Studies were performed with 250 μ m 15 N-labeled mNT in 50 m m Bis-Tris, pH 6.2, 100 m m NaCl at 298 K. A , mNT denaturation under aerobic

    Journal: The Journal of Biological Chemistry

    Article Title: Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster *

    doi: 10.1074/jbc.M115.711218

    Figure Lengend Snippet: Denaturation of oxidized holo-mNT under anaerobic conditions results in reduction of the remaining holo-mNT. Studies were performed with 250 μ m 15 N-labeled mNT in 50 m m Bis-Tris, pH 6.2, 100 m m NaCl at 298 K. A , mNT denaturation under aerobic

    Article Snippet: When specified, DTT was removed, and buffer was exchanged with 50 m m Bis-Tris, pH 6.2, 100 m m NaCl using a Micro Bio-Spin Size Exclusion column (Bio-Rad).

    Techniques: Labeling