Structured Review

Millipore m nacl
( a ) Size-exclusion chromatography peak of Nb_PrP_01 on Superdex 75 HR 10/300; the running buffer was 20 m M <t>Tris–HCl</t> pH 7.5, 150 m M <t>NaCl.</t> ( b ) SDS–PAGE of purified Nb_PrP_01 (15% polyacrylamide gel stained with Instant Blue).
M Nacl, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 128 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 128 article reviews
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Images

1) Product Images from "Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein"

Article Title: Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein

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

doi: 10.1107/S1744309110042168

( a ) Size-exclusion chromatography peak of Nb_PrP_01 on Superdex 75 HR 10/300; the running buffer was 20 m M Tris–HCl pH 7.5, 150 m M NaCl. ( b ) SDS–PAGE of purified Nb_PrP_01 (15% polyacrylamide gel stained with Instant Blue).
Figure Legend Snippet: ( a ) Size-exclusion chromatography peak of Nb_PrP_01 on Superdex 75 HR 10/300; the running buffer was 20 m M Tris–HCl pH 7.5, 150 m M NaCl. ( b ) SDS–PAGE of purified Nb_PrP_01 (15% polyacrylamide gel stained with Instant Blue).

Techniques Used: Size-exclusion Chromatography, SDS Page, Purification, Staining

2) Product Images from "A l-Lysine Transporter of High Stereoselectivity of the Amino Acid-Polyamine-Organocation (APC) Superfamily"

Article Title: A l-Lysine Transporter of High Stereoselectivity of the Amino Acid-Polyamine-Organocation (APC) Superfamily

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M113.510743

Titration calorimetry of STM2200 at 20 °C. A , l -lysine titration of 30 μ m STM2200 in 20 m m MES-NaOH, 0.025% (w/v) β-DDM (buffer B) containing 150 m m NaCl, pH 5.9 with 1 × 4 μl and 22 × 5.0 μl of
Figure Legend Snippet: Titration calorimetry of STM2200 at 20 °C. A , l -lysine titration of 30 μ m STM2200 in 20 m m MES-NaOH, 0.025% (w/v) β-DDM (buffer B) containing 150 m m NaCl, pH 5.9 with 1 × 4 μl and 22 × 5.0 μl of

Techniques Used: Titration

3) Product Images from "Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY"

Article Title: Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY

Journal: Acta crystallographica. Section D, Biological crystallography

doi:

Crystals contain intact NG-domain complex. ( a ) SDS–PAGE demonstrates that both proteins are present in the crystal. The crystallization drop was supplemented with mother liquor containing 5 mg ml −1 lysozyme as a wash control (arrow). A crystal was removed using a 100 µm nylon loop, passed through successive lysozyme-free mother-liquor washes and dissolved in water. The dissolved crystal and a sample of the crystallization mother liquor were analyzed by SDS–PAGE. The expected products are the intact Ffh NG domain (~33 kDa) and the proteolysis products of FtsY NG, migrating at ~22 and ~6 kDa. The crystal used in the experiment shown had a ‘sheaf’ morphology and was grown at 7 mg ml −1 under 1.7 M ammonium sulfate, 0.1 M MES pH 6.5, 1 m M SrCl 2 crystallization conditions. Similar experiments with other crystals ( e.g. having the ‘needle’ morphology) gave the same result. ( b ) Gel filtration demonstrates that the proteins are associated in a bona fide complex. The crystals were grown using protein at 7 mg ml −1 and 1.7 M ammonium sulfate, 0.1 M MES pH 6.5 crystallization conditions. The mother liquor was removed from the drop and the crystals were first washed with protein-free mother liquor and then dissolved in 2 µl of a mobile phase buffer, 50 m M HEPES, 50 m M NaCl, 2 m M MgCl 2 , supplemented with 1 m M ).
Figure Legend Snippet: Crystals contain intact NG-domain complex. ( a ) SDS–PAGE demonstrates that both proteins are present in the crystal. The crystallization drop was supplemented with mother liquor containing 5 mg ml −1 lysozyme as a wash control (arrow). A crystal was removed using a 100 µm nylon loop, passed through successive lysozyme-free mother-liquor washes and dissolved in water. The dissolved crystal and a sample of the crystallization mother liquor were analyzed by SDS–PAGE. The expected products are the intact Ffh NG domain (~33 kDa) and the proteolysis products of FtsY NG, migrating at ~22 and ~6 kDa. The crystal used in the experiment shown had a ‘sheaf’ morphology and was grown at 7 mg ml −1 under 1.7 M ammonium sulfate, 0.1 M MES pH 6.5, 1 m M SrCl 2 crystallization conditions. Similar experiments with other crystals ( e.g. having the ‘needle’ morphology) gave the same result. ( b ) Gel filtration demonstrates that the proteins are associated in a bona fide complex. The crystals were grown using protein at 7 mg ml −1 and 1.7 M ammonium sulfate, 0.1 M MES pH 6.5 crystallization conditions. The mother liquor was removed from the drop and the crystals were first washed with protein-free mother liquor and then dissolved in 2 µl of a mobile phase buffer, 50 m M HEPES, 50 m M NaCl, 2 m M MgCl 2 , supplemented with 1 m M ).

Techniques Used: SDS Page, Crystallization Assay, Filtration

4) Product Images from "The HtrA Protease from Streptococcus pneumoniae Digests Both Denatured Proteins and the Competence-stimulating Peptide *"

Article Title: The HtrA Protease from Streptococcus pneumoniae Digests Both Denatured Proteins and the Competence-stimulating Peptide *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M112.391482

Characterization of wild-type ( WT ) rHtrA and the S234A catalytic site variant. A , SDS-PAGE of samples in Tris/NaCl buffer following the preparative SEC step and after exchange into PBS. B , β-casein zymography. C , native gel electrophoresis. D
Figure Legend Snippet: Characterization of wild-type ( WT ) rHtrA and the S234A catalytic site variant. A , SDS-PAGE of samples in Tris/NaCl buffer following the preparative SEC step and after exchange into PBS. B , β-casein zymography. C , native gel electrophoresis. D

Techniques Used: Variant Assay, SDS Page, Size-exclusion Chromatography, Zymography, Nucleic Acid Electrophoresis

5) Product Images from "Folding of a Cyclin Box"

Article Title: Folding of a Cyclin Box

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M113.467316

RbAB particle size distribution at different GdmCl concentrations. Dynamic light scattering measurements of a 10 μ m RbAB solution in 20 m m phosphate buffer, pH 7.0, 200 m m NaCl, and 2 m m DTT with different GdmCl concentrations. The GdmCl concentration
Figure Legend Snippet: RbAB particle size distribution at different GdmCl concentrations. Dynamic light scattering measurements of a 10 μ m RbAB solution in 20 m m phosphate buffer, pH 7.0, 200 m m NaCl, and 2 m m DTT with different GdmCl concentrations. The GdmCl concentration

Techniques Used: Concentration Assay

6) Product Images from "N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *"

Article Title: N-terminal Cleaved Pancreatitis-associated Protein-III (PAP-III) Serves as a Scaffold for Neurites and Promotes Neurite Outgrowth *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M112.395301

Weak interactions of exogenously added ΔN-PAP-III fibers with glial cells. ΔN-PAP-III fibers produced in 25 m m Tris (pH 7.5) containing 150 m m NaCl were added to the culture media of astrocytes, microglia, and Schwann cells, and incubated
Figure Legend Snippet: Weak interactions of exogenously added ΔN-PAP-III fibers with glial cells. ΔN-PAP-III fibers produced in 25 m m Tris (pH 7.5) containing 150 m m NaCl were added to the culture media of astrocytes, microglia, and Schwann cells, and incubated

Techniques Used: Produced, Incubation

Association of exogenously added ΔN-PAP-III fibers with neurons. ΔN-PAP-III fibers produced in 25 m m Tris (pH 7.5) containing 150 m m NaCl were added to the culture media of primary cortical neurons precultured for 12–18 h. Twenty-four
Figure Legend Snippet: Association of exogenously added ΔN-PAP-III fibers with neurons. ΔN-PAP-III fibers produced in 25 m m Tris (pH 7.5) containing 150 m m NaCl were added to the culture media of primary cortical neurons precultured for 12–18 h. Twenty-four

Techniques Used: Produced

Precipitability of ΔN-PAP-III depends on Na + concentrations. A , PAP-III protein was incubated with (+) or without (−) trypsin in 25 m m Tris (pH 7.5) containing 0 (−), 25, and 150 m m NaCl for 2 h ( hrs ). B , PAP-III protein was treated
Figure Legend Snippet: Precipitability of ΔN-PAP-III depends on Na + concentrations. A , PAP-III protein was incubated with (+) or without (−) trypsin in 25 m m Tris (pH 7.5) containing 0 (−), 25, and 150 m m NaCl for 2 h ( hrs ). B , PAP-III protein was treated

Techniques Used: Incubation

Fibrillar structure of ΔN-PAP-III. A , PAP-III treated with trypsin in 25 m m Tris (pH 7.5) containing 0 (−), 25, and 150 m m NaCl was attached to PDL-coated coverslips and visualized by immunofluorescence using anti-PAP-III antibody. Scale
Figure Legend Snippet: Fibrillar structure of ΔN-PAP-III. A , PAP-III treated with trypsin in 25 m m Tris (pH 7.5) containing 0 (−), 25, and 150 m m NaCl was attached to PDL-coated coverslips and visualized by immunofluorescence using anti-PAP-III antibody. Scale

Techniques Used: Immunofluorescence

Related Articles

Ion Exchange Chromatography:

Article Title: Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY
Article Snippet: .. The complex between the two NG domains was formed by incubation of 15 µ M FtsY NG and 10 µ M Ffh NG in 50 m M HEPES pH 7.5, 2 m M MgCl2 , 50 m M NaCl and 1 m M β-γ-methyleneguanosine 5′-triphosphate (Sigma) in a 5 ml reaction mixture for 4 d at 310 K and the complex was purified by ion-exchange chromatography as described previously ( ). .. The presence of the intact complex was confirmed by gelfiltration chromatography.

Protease Inhibitor:

Article Title: Cross-talk between the Androgen Receptor and the Liver X Receptor
Article Snippet: .. Cells were harvested with SDS lysis buffer (1% (w/v) SDS, 10 m m Tris-HCl (pH 7.6), 100 m m NaCl), supplemented with 2% (v/v) protease inhibitor mixture (Sigma-Aldrich). .. Protein content was determined using the Pierce BCA protein assay.

Purification:

Article Title: Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein
Article Snippet: .. The nanobody was further purified by gel filtration on a Superdex 75 HR 10/30 column equilibrated in 20 m M Tris–HCl pH 7.5, 150 m M NaCl; fractions containing 99% pure nanobody were pooled and concentrated using an ultrafiltration unit (3000 molecular-weight cutoff, Millipore). .. The protein concentration was estimated from the A 280 as determined using a NanoDrop spectrophotometer (Thermo Scientific) using a value of 21 555.0 M −1 cm−1 for the extinction coefficient and the protein was stored at 277 K; 1 l of culture yielded 10 mg of pure protein (Fig. 1 ).

Article Title: Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY
Article Snippet: .. The complex between the two NG domains was formed by incubation of 15 µ M FtsY NG and 10 µ M Ffh NG in 50 m M HEPES pH 7.5, 2 m M MgCl2 , 50 m M NaCl and 1 m M β-γ-methyleneguanosine 5′-triphosphate (Sigma) in a 5 ml reaction mixture for 4 d at 310 K and the complex was purified by ion-exchange chromatography as described previously ( ). .. The presence of the intact complex was confirmed by gelfiltration chromatography.

Incubation:

Article Title: Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY
Article Snippet: .. The complex between the two NG domains was formed by incubation of 15 µ M FtsY NG and 10 µ M Ffh NG in 50 m M HEPES pH 7.5, 2 m M MgCl2 , 50 m M NaCl and 1 m M β-γ-methyleneguanosine 5′-triphosphate (Sigma) in a 5 ml reaction mixture for 4 d at 310 K and the complex was purified by ion-exchange chromatography as described previously ( ). .. The presence of the intact complex was confirmed by gelfiltration chromatography.

other:

Article Title: Folding of a Cyclin Box
Article Snippet: Unless stated otherwise, measurements were performed in 20 m m sodium phosphate buffer at pH 7.0, 200 m m NaCl, and 2 m m DTT at 20 ± 0.1 °C using analytical grade chemical reagents (Sigma-Aldrich or ICN).

Sonication:

Article Title: Structure of the Lipid Nanodisc-reconstituted Vacuolar ATPase Proton Channel
Article Snippet: .. E. coli total lipid extract (Avanti Polar Lipids) was suspended by sonication in disc-forming buffer (20 m m Tris-HCl (pH 7.4), 100 m m NaCl, and 0.5 m m EDTA) with the addition of 1 m m DTT (EMD Millipore). .. Detergent-solubilized Vo , purified MSP, and lipid were combined at a molar ratio of 0.02:1:25 with the addition of protease inhibitors, 1 m m PMSF, 1 m m leupeptin, 1 m m pepstatin, and 1 m m chymostatin (EMD Biosciences) and incubated at room temperature for 1 h with mixing.

Filtration:

Article Title: Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein
Article Snippet: .. The nanobody was further purified by gel filtration on a Superdex 75 HR 10/30 column equilibrated in 20 m M Tris–HCl pH 7.5, 150 m M NaCl; fractions containing 99% pure nanobody were pooled and concentrated using an ultrafiltration unit (3000 molecular-weight cutoff, Millipore). .. The protein concentration was estimated from the A 280 as determined using a NanoDrop spectrophotometer (Thermo Scientific) using a value of 21 555.0 M −1 cm−1 for the extinction coefficient and the protein was stored at 277 K; 1 l of culture yielded 10 mg of pure protein (Fig. 1 ).

Lysis:

Article Title: Cross-talk between the Androgen Receptor and the Liver X Receptor
Article Snippet: .. Cells were harvested with SDS lysis buffer (1% (w/v) SDS, 10 m m Tris-HCl (pH 7.6), 100 m m NaCl), supplemented with 2% (v/v) protease inhibitor mixture (Sigma-Aldrich). .. Protein content was determined using the Pierce BCA protein assay.

Molecular Weight:

Article Title: Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein
Article Snippet: .. The nanobody was further purified by gel filtration on a Superdex 75 HR 10/30 column equilibrated in 20 m M Tris–HCl pH 7.5, 150 m M NaCl; fractions containing 99% pure nanobody were pooled and concentrated using an ultrafiltration unit (3000 molecular-weight cutoff, Millipore). .. The protein concentration was estimated from the A 280 as determined using a NanoDrop spectrophotometer (Thermo Scientific) using a value of 21 555.0 M −1 cm−1 for the extinction coefficient and the protein was stored at 277 K; 1 l of culture yielded 10 mg of pure protein (Fig. 1 ).

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  • 92
    Millipore m nacl
    ( a ) Size-exclusion chromatography peak of Nb_PrP_01 on Superdex 75 HR 10/300; the running buffer was 20 m M <t>Tris–HCl</t> pH 7.5, 150 m M <t>NaCl.</t> ( b ) SDS–PAGE of purified Nb_PrP_01 (15% polyacrylamide gel stained with Instant Blue).
    M Nacl, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 128 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/m nacl/product/Millipore
    Average 92 stars, based on 128 article reviews
    Price from $9.99 to $1999.99
    m nacl - by Bioz Stars, 2021-01
    92/100 stars
      Buy from Supplier

    80
    Millipore m nacl gradient
    ( a ) Size-exclusion chromatography peak of Nb_PrP_01 on Superdex 75 HR 10/300; the running buffer was 20 m M <t>Tris–HCl</t> pH 7.5, 150 m M <t>NaCl.</t> ( b ) SDS–PAGE of purified Nb_PrP_01 (15% polyacrylamide gel stained with Instant Blue).
    M Nacl Gradient, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 0 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/m nacl gradient/product/Millipore
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    m nacl gradient - by Bioz Stars, 2021-01
    80/100 stars
      Buy from Supplier

    Image Search Results


    ( a ) Size-exclusion chromatography peak of Nb_PrP_01 on Superdex 75 HR 10/300; the running buffer was 20 m M Tris–HCl pH 7.5, 150 m M NaCl. ( b ) SDS–PAGE of purified Nb_PrP_01 (15% polyacrylamide gel stained with Instant Blue).

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

    Article Title: Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein

    doi: 10.1107/S1744309110042168

    Figure Lengend Snippet: ( a ) Size-exclusion chromatography peak of Nb_PrP_01 on Superdex 75 HR 10/300; the running buffer was 20 m M Tris–HCl pH 7.5, 150 m M NaCl. ( b ) SDS–PAGE of purified Nb_PrP_01 (15% polyacrylamide gel stained with Instant Blue).

    Article Snippet: The nanobody was further purified by gel filtration on a Superdex 75 HR 10/30 column equilibrated in 20 m M Tris–HCl pH 7.5, 150 m M NaCl; fractions containing 99% pure nanobody were pooled and concentrated using an ultrafiltration unit (3000 molecular-weight cutoff, Millipore).

    Techniques: Size-exclusion Chromatography, SDS Page, Purification, Staining