supernuclease  (Sino Biological)


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    Structured Review

    Sino Biological supernuclease
    ATP hydrolysis inhibits the formation of the RecA-saturated nucleofilaments and increases the dynamics from nucleation to extension. ( a ) CE-LIF electropherograms of the reaction mixtures of TMR-T 18 (10 n M ) and RecA protein (16.0 μ M ), showing the formation of six distinct RecA-TMR-T 18 complexes induced by ATP hydrolysis. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( b ) CE-LIFP electropherograms of the reaction mixtures of TMR-ss83mer (10 n M ) and RecA (3.0 μ M ), showing the formation of three types of RecA nucleofilaments in the presence of ATP. Peaks 1–3 represent the lightly assembled, moderately assembled and RecA-saturated nucleofilaments, respectively. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( c ) The relative abundance of the three types of RecA-TMR-ss83mer filaments is dependent on ATP concentration. ( d ) Denaturing PAGE analysis of time-dependent products of <t>supernuclease</t> digestion of the Cy5-ss83mer (20 n M ) and the reaction mixtures of Cy5-ss83mer (20 n M ), RecA (3.0 μ M ) and one nucleotide cofactor as indicated. M indicates ssDNA size markers with a unit of nucleotides (nts). The reactions proceeded at 37 °C for 10 min.
    Supernuclease, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/supernuclease/product/Sino Biological
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    supernuclease - by Bioz Stars, 2021-02
    93/100 stars

    Images

    1) Product Images from "ATPase activity tightly regulates RecA nucleofilaments to promote homologous recombination"

    Article Title: ATPase activity tightly regulates RecA nucleofilaments to promote homologous recombination

    Journal: Cell Discovery

    doi: 10.1038/celldisc.2016.53

    ATP hydrolysis inhibits the formation of the RecA-saturated nucleofilaments and increases the dynamics from nucleation to extension. ( a ) CE-LIF electropherograms of the reaction mixtures of TMR-T 18 (10 n M ) and RecA protein (16.0 μ M ), showing the formation of six distinct RecA-TMR-T 18 complexes induced by ATP hydrolysis. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( b ) CE-LIFP electropherograms of the reaction mixtures of TMR-ss83mer (10 n M ) and RecA (3.0 μ M ), showing the formation of three types of RecA nucleofilaments in the presence of ATP. Peaks 1–3 represent the lightly assembled, moderately assembled and RecA-saturated nucleofilaments, respectively. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( c ) The relative abundance of the three types of RecA-TMR-ss83mer filaments is dependent on ATP concentration. ( d ) Denaturing PAGE analysis of time-dependent products of supernuclease digestion of the Cy5-ss83mer (20 n M ) and the reaction mixtures of Cy5-ss83mer (20 n M ), RecA (3.0 μ M ) and one nucleotide cofactor as indicated. M indicates ssDNA size markers with a unit of nucleotides (nts). The reactions proceeded at 37 °C for 10 min.
    Figure Legend Snippet: ATP hydrolysis inhibits the formation of the RecA-saturated nucleofilaments and increases the dynamics from nucleation to extension. ( a ) CE-LIF electropherograms of the reaction mixtures of TMR-T 18 (10 n M ) and RecA protein (16.0 μ M ), showing the formation of six distinct RecA-TMR-T 18 complexes induced by ATP hydrolysis. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( b ) CE-LIFP electropherograms of the reaction mixtures of TMR-ss83mer (10 n M ) and RecA (3.0 μ M ), showing the formation of three types of RecA nucleofilaments in the presence of ATP. Peaks 1–3 represent the lightly assembled, moderately assembled and RecA-saturated nucleofilaments, respectively. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( c ) The relative abundance of the three types of RecA-TMR-ss83mer filaments is dependent on ATP concentration. ( d ) Denaturing PAGE analysis of time-dependent products of supernuclease digestion of the Cy5-ss83mer (20 n M ) and the reaction mixtures of Cy5-ss83mer (20 n M ), RecA (3.0 μ M ) and one nucleotide cofactor as indicated. M indicates ssDNA size markers with a unit of nucleotides (nts). The reactions proceeded at 37 °C for 10 min.

    Techniques Used: Concentration Assay, Polyacrylamide Gel Electrophoresis

    2) Product Images from "Rapid porcine corneal decellularization through the use of sodium N-lauroyl glutamate and supernuclease"

    Article Title: Rapid porcine corneal decellularization through the use of sodium N-lauroyl glutamate and supernuclease

    Journal: Journal of Tissue Engineering

    doi: 10.1177/2041731419875876

    Cytotoxicity, cytocompatibility, and biocompatibility examinations of porcine corneal stroma decellularized with SLG and supernuclease: (a) The proliferation curve of HECEs during 6 days’ cultivation in normal or conditioned culture medium ( n = 3 per group). (b) SEM micrographs of HCECs at 3 days after the cultivation on the surface of a DPC ( n = 3). (c) Rabbit corneal micropocket implantation results and (d) rabbit anterior chamber implantation results at 10 days postoperation ( n = 3 per group).
    Figure Legend Snippet: Cytotoxicity, cytocompatibility, and biocompatibility examinations of porcine corneal stroma decellularized with SLG and supernuclease: (a) The proliferation curve of HECEs during 6 days’ cultivation in normal or conditioned culture medium ( n = 3 per group). (b) SEM micrographs of HCECs at 3 days after the cultivation on the surface of a DPC ( n = 3). (c) Rabbit corneal micropocket implantation results and (d) rabbit anterior chamber implantation results at 10 days postoperation ( n = 3 per group).

    Techniques Used:

    Lamellar transplantation with porcine corneal stroma decellularized with SLG and supernuclease in rabbits: (a) Corneal re-epithelialization results detected by fluorescence staining at 1, 7, and 9 days after transplantation. (b) General appearance of eyes examined by slit lamp at 1, 7, and 28 days after transplantation. (c) OCT photographs of normal and decellularized corneal stroma at 7 days after transplantation. (d) H E staining of the DPCs at 14 and 28 days after transplantation. (e) Confocal microscopy photographs of DPCs at 4 months after transplantation.
    Figure Legend Snippet: Lamellar transplantation with porcine corneal stroma decellularized with SLG and supernuclease in rabbits: (a) Corneal re-epithelialization results detected by fluorescence staining at 1, 7, and 9 days after transplantation. (b) General appearance of eyes examined by slit lamp at 1, 7, and 28 days after transplantation. (c) OCT photographs of normal and decellularized corneal stroma at 7 days after transplantation. (d) H E staining of the DPCs at 14 and 28 days after transplantation. (e) Confocal microscopy photographs of DPCs at 4 months after transplantation.

    Techniques Used: Transplantation Assay, Fluorescence, Staining, Confocal Microscopy

    Related Articles

    Protein Purification:

    Article Title: Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3
    Article Snippet: .. Protein purification Cells were thawed in Buffer A (50 mM HEPES pH 7.5, 150 mM NaCl, 1 mM TCEP (Thermo Fisher), 5% glycerol) supplemented with 1 Complete Protease Inhibitor (EDTA-free) tablet (Roche), 70 µg RNAse A (Roche), and 100 U ml−1 Supernuclease (Sino Biological) and then lysed by sonication. .. Following sonication, cell lysate was supplemented with 1 mM PMSF (Sigma).

    Article Title: ATP dependent DNA transport within cohesin: Scc2 clamps DNA on top of engaged heads while Scc3 promotes entrapment within the SMC-kleisin ring
    Article Snippet: .. Protein purification Cells were thawed in Buffer A (50 mM HEPES pH 7.5, 150 mM NaCl, 1 mM TCEP (Thermo Fisher), 5% glycerol) supplemented with 1 Complete Protease Inhibitor (EDTA-free) tablet (Roche), 70 µg RNAse A (Roche), and 100 U ml-1 Supernuclease (Sino Biological) and then lysed by sonication. .. Following sonication, cell lysate was supplemented with 1 mM PMSF (Sigma).

    Protease Inhibitor:

    Article Title: Cellular N-myristoyltransferases play a crucial picornavirus genus-specific role in viral assembly, virion maturation, and infectivity
    Article Snippet: .. DNase I, RNase A and EDTA-free complete protease inhibitor cocktail were from Roche, SuperNuclease was obtained from SinoBiological and InstantBlue from Expedon. .. 2-hydroxy-myristate (2-HMA) was obtained from Enzo Life Sciences; a 10 mM stock solution was prepared in DMSO and kept at –20°C.

    Article Title: Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3
    Article Snippet: .. Protein purification Cells were thawed in Buffer A (50 mM HEPES pH 7.5, 150 mM NaCl, 1 mM TCEP (Thermo Fisher), 5% glycerol) supplemented with 1 Complete Protease Inhibitor (EDTA-free) tablet (Roche), 70 µg RNAse A (Roche), and 100 U ml−1 Supernuclease (Sino Biological) and then lysed by sonication. .. Following sonication, cell lysate was supplemented with 1 mM PMSF (Sigma).

    Article Title: ATP dependent DNA transport within cohesin: Scc2 clamps DNA on top of engaged heads while Scc3 promotes entrapment within the SMC-kleisin ring
    Article Snippet: .. Protein purification Cells were thawed in Buffer A (50 mM HEPES pH 7.5, 150 mM NaCl, 1 mM TCEP (Thermo Fisher), 5% glycerol) supplemented with 1 Complete Protease Inhibitor (EDTA-free) tablet (Roche), 70 µg RNAse A (Roche), and 100 U ml-1 Supernuclease (Sino Biological) and then lysed by sonication. .. Following sonication, cell lysate was supplemented with 1 mM PMSF (Sigma).

    Centrifugation:

    Article Title: Elongation/Termination Factor Exchange Mediated by PP1 Phosphatase Orchestrates Transcription Termination
    Article Snippet: .. Cells from 12L were collected by centrifugation at 6000 g, 4°C for 15 min. Pellets were resuspended in NiTA buffer (50 mM Tris-HCl pH 7.8, 500 mM NaCl, 5 mM imidazole, 1 mM 2-mercaptoethanol) supplemented with 2500 U of SuperNuclease (Sino Biological Inc.). .. Cells were incubated for 20 min at 4 °C, lysed by French Press at 20 kpsi and then 0.5% Tween and 1mM PMSF were added.

    other:

    Article Title: Rapid porcine corneal decellularization through the use of sodium N-lauroyl glutamate and supernuclease
    Article Snippet: Preparation of DPCIn order to compare the decellularization effects of detergents, the porcine corneal stroma was separately treated with 0.5% SLG (Sigma-Aldrich, St. Louis, MO, USA), SLS (Sigma-Aldrich), SDS (Solarbio, Beijing, China), or Triton X-100 (Solarbio), supplemented with 200 U/mL supernuclease (Sino Biological, Beijing, China) in PBS for 2 h at room temperature under shaking condition (100 r/min).

    Sonication:

    Article Title: Transport of DNA within cohesin involves clamping on top of engaged heads by Scc2 and entrapment within the ring by Scc3
    Article Snippet: .. Protein purification Cells were thawed in Buffer A (50 mM HEPES pH 7.5, 150 mM NaCl, 1 mM TCEP (Thermo Fisher), 5% glycerol) supplemented with 1 Complete Protease Inhibitor (EDTA-free) tablet (Roche), 70 µg RNAse A (Roche), and 100 U ml−1 Supernuclease (Sino Biological) and then lysed by sonication. .. Following sonication, cell lysate was supplemented with 1 mM PMSF (Sigma).

    Article Title: ATP dependent DNA transport within cohesin: Scc2 clamps DNA on top of engaged heads while Scc3 promotes entrapment within the SMC-kleisin ring
    Article Snippet: .. Protein purification Cells were thawed in Buffer A (50 mM HEPES pH 7.5, 150 mM NaCl, 1 mM TCEP (Thermo Fisher), 5% glycerol) supplemented with 1 Complete Protease Inhibitor (EDTA-free) tablet (Roche), 70 µg RNAse A (Roche), and 100 U ml-1 Supernuclease (Sino Biological) and then lysed by sonication. .. Following sonication, cell lysate was supplemented with 1 mM PMSF (Sigma).

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  • 93
    Sino Biological supernuclease
    ATP hydrolysis inhibits the formation of the RecA-saturated nucleofilaments and increases the dynamics from nucleation to extension. ( a ) CE-LIF electropherograms of the reaction mixtures of TMR-T 18 (10 n M ) and RecA protein (16.0 μ M ), showing the formation of six distinct RecA-TMR-T 18 complexes induced by ATP hydrolysis. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( b ) CE-LIFP electropherograms of the reaction mixtures of TMR-ss83mer (10 n M ) and RecA (3.0 μ M ), showing the formation of three types of RecA nucleofilaments in the presence of ATP. Peaks 1–3 represent the lightly assembled, moderately assembled and RecA-saturated nucleofilaments, respectively. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( c ) The relative abundance of the three types of RecA-TMR-ss83mer filaments is dependent on ATP concentration. ( d ) Denaturing PAGE analysis of time-dependent products of <t>supernuclease</t> digestion of the Cy5-ss83mer (20 n M ) and the reaction mixtures of Cy5-ss83mer (20 n M ), RecA (3.0 μ M ) and one nucleotide cofactor as indicated. M indicates ssDNA size markers with a unit of nucleotides (nts). The reactions proceeded at 37 °C for 10 min.
    Supernuclease, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/supernuclease/product/Sino Biological
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    supernuclease - by Bioz Stars, 2021-02
    93/100 stars
      Buy from Supplier

    Image Search Results


    ATP hydrolysis inhibits the formation of the RecA-saturated nucleofilaments and increases the dynamics from nucleation to extension. ( a ) CE-LIF electropherograms of the reaction mixtures of TMR-T 18 (10 n M ) and RecA protein (16.0 μ M ), showing the formation of six distinct RecA-TMR-T 18 complexes induced by ATP hydrolysis. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( b ) CE-LIFP electropherograms of the reaction mixtures of TMR-ss83mer (10 n M ) and RecA (3.0 μ M ), showing the formation of three types of RecA nucleofilaments in the presence of ATP. Peaks 1–3 represent the lightly assembled, moderately assembled and RecA-saturated nucleofilaments, respectively. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( c ) The relative abundance of the three types of RecA-TMR-ss83mer filaments is dependent on ATP concentration. ( d ) Denaturing PAGE analysis of time-dependent products of supernuclease digestion of the Cy5-ss83mer (20 n M ) and the reaction mixtures of Cy5-ss83mer (20 n M ), RecA (3.0 μ M ) and one nucleotide cofactor as indicated. M indicates ssDNA size markers with a unit of nucleotides (nts). The reactions proceeded at 37 °C for 10 min.

    Journal: Cell Discovery

    Article Title: ATPase activity tightly regulates RecA nucleofilaments to promote homologous recombination

    doi: 10.1038/celldisc.2016.53

    Figure Lengend Snippet: ATP hydrolysis inhibits the formation of the RecA-saturated nucleofilaments and increases the dynamics from nucleation to extension. ( a ) CE-LIF electropherograms of the reaction mixtures of TMR-T 18 (10 n M ) and RecA protein (16.0 μ M ), showing the formation of six distinct RecA-TMR-T 18 complexes induced by ATP hydrolysis. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( b ) CE-LIFP electropherograms of the reaction mixtures of TMR-ss83mer (10 n M ) and RecA (3.0 μ M ), showing the formation of three types of RecA nucleofilaments in the presence of ATP. Peaks 1–3 represent the lightly assembled, moderately assembled and RecA-saturated nucleofilaments, respectively. The Y axis of the bottom trace can be applied to all stacked traces in the panel. ( c ) The relative abundance of the three types of RecA-TMR-ss83mer filaments is dependent on ATP concentration. ( d ) Denaturing PAGE analysis of time-dependent products of supernuclease digestion of the Cy5-ss83mer (20 n M ) and the reaction mixtures of Cy5-ss83mer (20 n M ), RecA (3.0 μ M ) and one nucleotide cofactor as indicated. M indicates ssDNA size markers with a unit of nucleotides (nts). The reactions proceeded at 37 °C for 10 min.

    Article Snippet: Supernuclease was obtained from Sino Biological Inc. (Beijing, China).

    Techniques: Concentration Assay, Polyacrylamide Gel Electrophoresis

    Cytotoxicity, cytocompatibility, and biocompatibility examinations of porcine corneal stroma decellularized with SLG and supernuclease: (a) The proliferation curve of HECEs during 6 days’ cultivation in normal or conditioned culture medium ( n = 3 per group). (b) SEM micrographs of HCECs at 3 days after the cultivation on the surface of a DPC ( n = 3). (c) Rabbit corneal micropocket implantation results and (d) rabbit anterior chamber implantation results at 10 days postoperation ( n = 3 per group).

    Journal: Journal of Tissue Engineering

    Article Title: Rapid porcine corneal decellularization through the use of sodium N-lauroyl glutamate and supernuclease

    doi: 10.1177/2041731419875876

    Figure Lengend Snippet: Cytotoxicity, cytocompatibility, and biocompatibility examinations of porcine corneal stroma decellularized with SLG and supernuclease: (a) The proliferation curve of HECEs during 6 days’ cultivation in normal or conditioned culture medium ( n = 3 per group). (b) SEM micrographs of HCECs at 3 days after the cultivation on the surface of a DPC ( n = 3). (c) Rabbit corneal micropocket implantation results and (d) rabbit anterior chamber implantation results at 10 days postoperation ( n = 3 per group).

    Article Snippet: Preparation of DPCIn order to compare the decellularization effects of detergents, the porcine corneal stroma was separately treated with 0.5% SLG (Sigma-Aldrich, St. Louis, MO, USA), SLS (Sigma-Aldrich), SDS (Solarbio, Beijing, China), or Triton X-100 (Solarbio), supplemented with 200 U/mL supernuclease (Sino Biological, Beijing, China) in PBS for 2 h at room temperature under shaking condition (100 r/min).

    Techniques:

    Lamellar transplantation with porcine corneal stroma decellularized with SLG and supernuclease in rabbits: (a) Corneal re-epithelialization results detected by fluorescence staining at 1, 7, and 9 days after transplantation. (b) General appearance of eyes examined by slit lamp at 1, 7, and 28 days after transplantation. (c) OCT photographs of normal and decellularized corneal stroma at 7 days after transplantation. (d) H E staining of the DPCs at 14 and 28 days after transplantation. (e) Confocal microscopy photographs of DPCs at 4 months after transplantation.

    Journal: Journal of Tissue Engineering

    Article Title: Rapid porcine corneal decellularization through the use of sodium N-lauroyl glutamate and supernuclease

    doi: 10.1177/2041731419875876

    Figure Lengend Snippet: Lamellar transplantation with porcine corneal stroma decellularized with SLG and supernuclease in rabbits: (a) Corneal re-epithelialization results detected by fluorescence staining at 1, 7, and 9 days after transplantation. (b) General appearance of eyes examined by slit lamp at 1, 7, and 28 days after transplantation. (c) OCT photographs of normal and decellularized corneal stroma at 7 days after transplantation. (d) H E staining of the DPCs at 14 and 28 days after transplantation. (e) Confocal microscopy photographs of DPCs at 4 months after transplantation.

    Article Snippet: Preparation of DPCIn order to compare the decellularization effects of detergents, the porcine corneal stroma was separately treated with 0.5% SLG (Sigma-Aldrich, St. Louis, MO, USA), SLS (Sigma-Aldrich), SDS (Solarbio, Beijing, China), or Triton X-100 (Solarbio), supplemented with 200 U/mL supernuclease (Sino Biological, Beijing, China) in PBS for 2 h at room temperature under shaking condition (100 r/min).

    Techniques: Transplantation Assay, Fluorescence, Staining, Confocal Microscopy