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Roche mgcl₂
Mgcl₂, supplied by Roche, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mgcl₂/product/Roche
Average 85 stars, based on 1 article reviews
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mgcl₂ - by Bioz Stars, 2020-07
85/100 stars

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Polymerase Chain Reaction:

Article Title: Expression and Antigenic Evaluation of VacA Antigenic Fragment of Helicobacter Pylori
Article Snippet: .. PCR amplification was performed in a 50 μl total volume containing 3 μl of template DNA, 2 μl of each primers (10 picomole), 8 μl MgCl₂ (25 mM), 1.5 μl dNTP mixture, 5 μl PCR buffer (10X) and 1 μl of expand DNA polymerase (Roche, Germany). .. The following conditions were used for amplification: initial denaturation at 94°C for 5 min followed by 30 cycles of denaturation at 94°C for 1 min, annealing at 53°C for 1 min and extension at 72°C for 1 min and further extension for 5 min at 72°C ( ).

Amplification:

Article Title: Expression and Antigenic Evaluation of VacA Antigenic Fragment of Helicobacter Pylori
Article Snippet: .. PCR amplification was performed in a 50 μl total volume containing 3 μl of template DNA, 2 μl of each primers (10 picomole), 8 μl MgCl₂ (25 mM), 1.5 μl dNTP mixture, 5 μl PCR buffer (10X) and 1 μl of expand DNA polymerase (Roche, Germany). .. The following conditions were used for amplification: initial denaturation at 94°C for 5 min followed by 30 cycles of denaturation at 94°C for 1 min, annealing at 53°C for 1 min and extension at 72°C for 1 min and further extension for 5 min at 72°C ( ).

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  • mgcl  (Roche)
    93
    Roche mgcl
    Development of hydrolysis resistant hSTING agonists ( a ) Scheme of enzymatic synthesis of 3′3′-cGAMP and 2′3′-cGAMP analogs. For 3′3′-cGAMP, 50 nM of DncV was incubated with 1 mM ATP and 1 mM GTP in 1 mL buffer containing 20 mM <t>Tris-HCl,</t> pH 8.0, 20 mM <t>MgCl</t> 2 for 3 h at room temperature. For 2′3′-cGAMP analogs, 1-10 μM mouse cGAS (amino acid residues 147-507) was incubated with 1 mM ATP, 1 mM GTP, and 0.1 mg/mL HT-DNA in 1 mL of the same buffer for 12 h at room temperature. ( b ) Hydrolysis reactions of ENPP1 (1 nM) with the analogs (10 μM). ( c ) Scintillation proximity assay to measure the binding affinity of the analogs towards hSTING (amino acid residues 139-379). Biotinylated hSTING (100 nM) was immobilized onto 96-well streptavidin coated SPA plates. Neat 35 S-labeled 2′3′-cGA s MP (500 pM) was used as the probe. N=3 samples. Data are presented as mean and standard error. ( d ) IFN-β production in THP-1 cells stimulated with the analogs. THP-1 cells were incubated with the analogs at the indicated concentrations for 24 h. IFN-β in the media was measured using a HEK-SEAP cell line. Representative data from a biological triplicate is depicted.
    Mgcl, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mgcl/product/Roche
    Average 93 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
    mgcl - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    89
    Roche co immunoprecipitation buffer
    Isolation of intestinal brush-border protein complexes Murine intestinal BBMVs were prepared using MgCl 2 precipitation and centrifugation. ( A ) BBMVs (50 μg/sample) at 1 mg/ml were solubilized in detergent buffer as indicated and mixed with Coomassie Brilliant Blue G-250 loading dye before separation. Samples were separated by Blue native PAGE. Following semi-dry transfer on to a PVDF membrane, individual proteins were detected by immunoblot analysis. The blot was stripped and re-probed for the proteins indicated, to allow a direct comparison of band positions. Protein complexes and individual proteins are numbered 1–7 (discussed in the main text). ( B ) Murine BBMVs were solubilized in <t>co-immunoprecipitation</t> buffer, followed by incubation with Protein A and primary antibodies against either B 0 AT1 or APN. After overnight incubation of BBMV samples, the cleared lysate and intestinal homogenate were separated by SDS/PAGE. Following semi-dry transfer on to a nitrocellulose membrane, the blots were pre-stripped using stripping buffer and blocked overnight to reduce background signal. Individual proteins were then detected as indicated above the blot and visualized using immunoblot analysis. Molecular masses are indicated to the left-hand side in kDa.
    Co Immunoprecipitation Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 89/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/co immunoprecipitation buffer/product/Roche
    Average 89 stars, based on 10 article reviews
    Price from $9.99 to $1999.99
    co immunoprecipitation buffer - by Bioz Stars, 2020-07
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    94
    Roche pcr buffer
    Isolation of intestinal brush-border protein complexes Murine intestinal BBMVs were prepared using MgCl 2 precipitation and centrifugation. ( A ) BBMVs (50 μg/sample) at 1 mg/ml were solubilized in detergent buffer as indicated and mixed with Coomassie Brilliant Blue G-250 loading dye before separation. Samples were separated by Blue native PAGE. Following semi-dry transfer on to a PVDF membrane, individual proteins were detected by immunoblot analysis. The blot was stripped and re-probed for the proteins indicated, to allow a direct comparison of band positions. Protein complexes and individual proteins are numbered 1–7 (discussed in the main text). ( B ) Murine BBMVs were solubilized in <t>co-immunoprecipitation</t> buffer, followed by incubation with Protein A and primary antibodies against either B 0 AT1 or APN. After overnight incubation of BBMV samples, the cleared lysate and intestinal homogenate were separated by SDS/PAGE. Following semi-dry transfer on to a nitrocellulose membrane, the blots were pre-stripped using stripping buffer and blocked overnight to reduce background signal. Individual proteins were then detected as indicated above the blot and visualized using immunoblot analysis. Molecular masses are indicated to the left-hand side in kDa.
    Pcr Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 94/100, based on 905 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pcr buffer/product/Roche
    Average 94 stars, based on 905 article reviews
    Price from $9.99 to $1999.99
    pcr buffer - by Bioz Stars, 2020-07
    94/100 stars
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    Development of hydrolysis resistant hSTING agonists ( a ) Scheme of enzymatic synthesis of 3′3′-cGAMP and 2′3′-cGAMP analogs. For 3′3′-cGAMP, 50 nM of DncV was incubated with 1 mM ATP and 1 mM GTP in 1 mL buffer containing 20 mM Tris-HCl, pH 8.0, 20 mM MgCl 2 for 3 h at room temperature. For 2′3′-cGAMP analogs, 1-10 μM mouse cGAS (amino acid residues 147-507) was incubated with 1 mM ATP, 1 mM GTP, and 0.1 mg/mL HT-DNA in 1 mL of the same buffer for 12 h at room temperature. ( b ) Hydrolysis reactions of ENPP1 (1 nM) with the analogs (10 μM). ( c ) Scintillation proximity assay to measure the binding affinity of the analogs towards hSTING (amino acid residues 139-379). Biotinylated hSTING (100 nM) was immobilized onto 96-well streptavidin coated SPA plates. Neat 35 S-labeled 2′3′-cGA s MP (500 pM) was used as the probe. N=3 samples. Data are presented as mean and standard error. ( d ) IFN-β production in THP-1 cells stimulated with the analogs. THP-1 cells were incubated with the analogs at the indicated concentrations for 24 h. IFN-β in the media was measured using a HEK-SEAP cell line. Representative data from a biological triplicate is depicted.

    Journal: Nature chemical biology

    Article Title: Hydrolysis of 2′3′-cGAMP by ENPP1 and design of non-hydrolyzable analogs

    doi: 10.1038/nchembio.1661

    Figure Lengend Snippet: Development of hydrolysis resistant hSTING agonists ( a ) Scheme of enzymatic synthesis of 3′3′-cGAMP and 2′3′-cGAMP analogs. For 3′3′-cGAMP, 50 nM of DncV was incubated with 1 mM ATP and 1 mM GTP in 1 mL buffer containing 20 mM Tris-HCl, pH 8.0, 20 mM MgCl 2 for 3 h at room temperature. For 2′3′-cGAMP analogs, 1-10 μM mouse cGAS (amino acid residues 147-507) was incubated with 1 mM ATP, 1 mM GTP, and 0.1 mg/mL HT-DNA in 1 mL of the same buffer for 12 h at room temperature. ( b ) Hydrolysis reactions of ENPP1 (1 nM) with the analogs (10 μM). ( c ) Scintillation proximity assay to measure the binding affinity of the analogs towards hSTING (amino acid residues 139-379). Biotinylated hSTING (100 nM) was immobilized onto 96-well streptavidin coated SPA plates. Neat 35 S-labeled 2′3′-cGA s MP (500 pM) was used as the probe. N=3 samples. Data are presented as mean and standard error. ( d ) IFN-β production in THP-1 cells stimulated with the analogs. THP-1 cells were incubated with the analogs at the indicated concentrations for 24 h. IFN-β in the media was measured using a HEK-SEAP cell line. Representative data from a biological triplicate is depicted.

    Article Snippet: Preparation of cell and tissue extracts To determine whether THP-1 cells, L929 cells, and MDA-MB231 possess hydrolase activity for 2′3′-cGAMP, the whole cell lysate was generated using lysis buffer:10 mM Tris-HCl, pH 7.5,150 mM NaCl, 1% NP-40, 1.5 mM MgCl, 2 mM DTT, protease inhibitor tablet (Roche) at 1 mL for 100 million cells.

    Techniques: Incubation, Scintillation Proximity Assay, Binding Assay, Labeling

    Isolation of intestinal brush-border protein complexes Murine intestinal BBMVs were prepared using MgCl 2 precipitation and centrifugation. ( A ) BBMVs (50 μg/sample) at 1 mg/ml were solubilized in detergent buffer as indicated and mixed with Coomassie Brilliant Blue G-250 loading dye before separation. Samples were separated by Blue native PAGE. Following semi-dry transfer on to a PVDF membrane, individual proteins were detected by immunoblot analysis. The blot was stripped and re-probed for the proteins indicated, to allow a direct comparison of band positions. Protein complexes and individual proteins are numbered 1–7 (discussed in the main text). ( B ) Murine BBMVs were solubilized in co-immunoprecipitation buffer, followed by incubation with Protein A and primary antibodies against either B 0 AT1 or APN. After overnight incubation of BBMV samples, the cleared lysate and intestinal homogenate were separated by SDS/PAGE. Following semi-dry transfer on to a nitrocellulose membrane, the blots were pre-stripped using stripping buffer and blocked overnight to reduce background signal. Individual proteins were then detected as indicated above the blot and visualized using immunoblot analysis. Molecular masses are indicated to the left-hand side in kDa.

    Journal: Biochemical Journal

    Article Title: Intestinal peptidases form functional complexes with the neutral amino acid transporter B0AT1

    doi: 10.1042/BJ20120307

    Figure Lengend Snippet: Isolation of intestinal brush-border protein complexes Murine intestinal BBMVs were prepared using MgCl 2 precipitation and centrifugation. ( A ) BBMVs (50 μg/sample) at 1 mg/ml were solubilized in detergent buffer as indicated and mixed with Coomassie Brilliant Blue G-250 loading dye before separation. Samples were separated by Blue native PAGE. Following semi-dry transfer on to a PVDF membrane, individual proteins were detected by immunoblot analysis. The blot was stripped and re-probed for the proteins indicated, to allow a direct comparison of band positions. Protein complexes and individual proteins are numbered 1–7 (discussed in the main text). ( B ) Murine BBMVs were solubilized in co-immunoprecipitation buffer, followed by incubation with Protein A and primary antibodies against either B 0 AT1 or APN. After overnight incubation of BBMV samples, the cleared lysate and intestinal homogenate were separated by SDS/PAGE. Following semi-dry transfer on to a nitrocellulose membrane, the blots were pre-stripped using stripping buffer and blocked overnight to reduce background signal. Individual proteins were then detected as indicated above the blot and visualized using immunoblot analysis. Molecular masses are indicated to the left-hand side in kDa.

    Article Snippet: Co-immunoprecipitation of membrane proteins For co-immunoprecipitations, 150–300 μg of BBMVs were solubilized for 1 h at 1 μg/μl in co-immunoprecipitation buffer [20 mM Tris, pH 7.4, 150 mM NaCl, 5 mM MgCl and 1% (v/v) Triton X-100] containing the Complete™ EDTA-free protease inhibitor cocktail (Roche Diagnostics).

    Techniques: Isolation, Centrifugation, Blue Native PAGE, Immunoprecipitation, Incubation, SDS Page, Stripping Membranes