bio atp  (Jena Bioscience)


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    Name:
    N6 6 Aminohexyl ATP Biotin
    Description:

    Catalog Number:
    NU-805-BIO
    Price:
    175.2
    Category:
    Nucleotides Nucleosides
    Size:
    50 µl
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    Structured Review

    Jena Bioscience bio atp
    dsDNA and CDN bind to the DEAD domain at the same sites. ( A ) Pull-down assays of DEAD, using bio-cGG in the presence of unlabeled <t>ISD</t> (left panel), and bio-ISD in the presence of unlabeled cGG (right panel). The final concentrations of unlabeled ISD or cGG are 0, 0.5, 1, 2 or 4 μM. ( B ) Pull-down assays of DEAD, using bio-ISD (left panel) or bio-cGG (right panel), in the presence of 1 mM unlabeled <t>ATP,</t> ADP or AMPPNP. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .

    https://www.bioz.com/result/bio atp/product/Jena Bioscience
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bio atp - by Bioz Stars, 2021-05
    88/100 stars

    Images

    1) Product Images from "Structural and Functional Analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide"

    Article Title: Structural and Functional Analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide

    Journal: Scientific Reports

    doi: 10.1038/srep34756

    dsDNA and CDN bind to the DEAD domain at the same sites. ( A ) Pull-down assays of DEAD, using bio-cGG in the presence of unlabeled ISD (left panel), and bio-ISD in the presence of unlabeled cGG (right panel). The final concentrations of unlabeled ISD or cGG are 0, 0.5, 1, 2 or 4 μM. ( B ) Pull-down assays of DEAD, using bio-ISD (left panel) or bio-cGG (right panel), in the presence of 1 mM unlabeled ATP, ADP or AMPPNP. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .
    Figure Legend Snippet: dsDNA and CDN bind to the DEAD domain at the same sites. ( A ) Pull-down assays of DEAD, using bio-cGG in the presence of unlabeled ISD (left panel), and bio-ISD in the presence of unlabeled cGG (right panel). The final concentrations of unlabeled ISD or cGG are 0, 0.5, 1, 2 or 4 μM. ( B ) Pull-down assays of DEAD, using bio-ISD (left panel) or bio-cGG (right panel), in the presence of 1 mM unlabeled ATP, ADP or AMPPNP. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .

    Techniques Used:

    Three forms of DDX41 reveal the structural rearrangement in the ATP-binding site. ( A ) Structure and sequence comparison between DDX41 and DDX3 (PDB ID: 5E7M). The Q motif and motif I of DDX3 are colored as in DDX41, whereas the other regions are colored silver. The amino-acid sequences of full-length DDX23 and DDX42 are the second and third most similar to that of DDX41. ( B ) Docking model of the DDX41 closed form bound to ATP (left panel), based on the DDX3-AMPPNP complex structure (PDB ID: 5E7M) (right panel). ( C ) Pull-down assays of the DEAD mutant, using bio-ATP and bio-AMPPNP. A cropped gel is shown. The full-length gel with the cropping lines indicated is shown in Figure S7 . ( D ) Docking models of the DDX41 open forms bound to ATP, based on the DDX3-AMPPNP complex structure (PDB ID: 5E7M). Models of the open form 1 (left panel) and the open form 2 (right panel) are shown.
    Figure Legend Snippet: Three forms of DDX41 reveal the structural rearrangement in the ATP-binding site. ( A ) Structure and sequence comparison between DDX41 and DDX3 (PDB ID: 5E7M). The Q motif and motif I of DDX3 are colored as in DDX41, whereas the other regions are colored silver. The amino-acid sequences of full-length DDX23 and DDX42 are the second and third most similar to that of DDX41. ( B ) Docking model of the DDX41 closed form bound to ATP (left panel), based on the DDX3-AMPPNP complex structure (PDB ID: 5E7M) (right panel). ( C ) Pull-down assays of the DEAD mutant, using bio-ATP and bio-AMPPNP. A cropped gel is shown. The full-length gel with the cropping lines indicated is shown in Figure S7 . ( D ) Docking models of the DDX41 open forms bound to ATP, based on the DDX3-AMPPNP complex structure (PDB ID: 5E7M). Models of the open form 1 (left panel) and the open form 2 (right panel) are shown.

    Techniques Used: Binding Assay, Sequencing, Mutagenesis

    The DDX41 DEAD domain binds to dsDNA and CDN. ( A ) FL-DDX41 and its truncated variants. DDX41 contains the DEAD domain (sky blue), the HELICc domain (orange) and the Zinc finger (ZF, gray). ( B ) Pull-down assays of DDX41, using bio-ISD (left panel) and bio-cGG (right panel). In all of the pull-down assays, the final concentration of bio-ISD, bio-cGG, bio-ATP or bio-AMPPNP is 1 μM, unless otherwise stated. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .
    Figure Legend Snippet: The DDX41 DEAD domain binds to dsDNA and CDN. ( A ) FL-DDX41 and its truncated variants. DDX41 contains the DEAD domain (sky blue), the HELICc domain (orange) and the Zinc finger (ZF, gray). ( B ) Pull-down assays of DDX41, using bio-ISD (left panel) and bio-cGG (right panel). In all of the pull-down assays, the final concentration of bio-ISD, bio-cGG, bio-ATP or bio-AMPPNP is 1 μM, unless otherwise stated. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .

    Techniques Used: Concentration Assay

    Related Articles

    Concentration Assay:

    Article Title: Structural and Functional Analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide
    Article Snippet: For negative controls and competition assays, unlabeled ATP, ADP, AMPPNP (SIGMA) and cGG (C057-01, BioLog) were used. .. Bio-ISD, bio-cGG (2′-O- (6-[biotinyl]aminohexylcarbamoyl)-cyclic diguanosine monophosphate, B098-001, BioLog), bio-ATP (N6 -(6-amino)hexyl-adenosine-5′-triphosphate-biotin, NU-805-BIO, Jena Bioscience) and bio-AMPPNP (2′/3′-O-(2-aminoethyl-carbamoyl)-adenosine-5′-[(β,γ)-imido] triphosphate-biotin, NU-810-BIO, Jena Bioscience), each at a final concentration of 1 μM, were incubated with Dynabeads M-280 Streptavidin (Thermo Fisher Scientific) for 30 min at 4 °C in binding buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10% glycerol, 0.5 mM EDTA, 1 mM 2-mercaptoethanol, 0.5% Nonidet P-40). .. The beads were washed with binding buffer three times, and then were incubated with the proteins for 1 h at 4 °C in binding buffer.

    Incubation:

    Article Title: Structural and Functional Analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide
    Article Snippet: For negative controls and competition assays, unlabeled ATP, ADP, AMPPNP (SIGMA) and cGG (C057-01, BioLog) were used. .. Bio-ISD, bio-cGG (2′-O- (6-[biotinyl]aminohexylcarbamoyl)-cyclic diguanosine monophosphate, B098-001, BioLog), bio-ATP (N6 -(6-amino)hexyl-adenosine-5′-triphosphate-biotin, NU-805-BIO, Jena Bioscience) and bio-AMPPNP (2′/3′-O-(2-aminoethyl-carbamoyl)-adenosine-5′-[(β,γ)-imido] triphosphate-biotin, NU-810-BIO, Jena Bioscience), each at a final concentration of 1 μM, were incubated with Dynabeads M-280 Streptavidin (Thermo Fisher Scientific) for 30 min at 4 °C in binding buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10% glycerol, 0.5 mM EDTA, 1 mM 2-mercaptoethanol, 0.5% Nonidet P-40). .. The beads were washed with binding buffer three times, and then were incubated with the proteins for 1 h at 4 °C in binding buffer.

    Binding Assay:

    Article Title: Structural and Functional Analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide
    Article Snippet: For negative controls and competition assays, unlabeled ATP, ADP, AMPPNP (SIGMA) and cGG (C057-01, BioLog) were used. .. Bio-ISD, bio-cGG (2′-O- (6-[biotinyl]aminohexylcarbamoyl)-cyclic diguanosine monophosphate, B098-001, BioLog), bio-ATP (N6 -(6-amino)hexyl-adenosine-5′-triphosphate-biotin, NU-805-BIO, Jena Bioscience) and bio-AMPPNP (2′/3′-O-(2-aminoethyl-carbamoyl)-adenosine-5′-[(β,γ)-imido] triphosphate-biotin, NU-810-BIO, Jena Bioscience), each at a final concentration of 1 μM, were incubated with Dynabeads M-280 Streptavidin (Thermo Fisher Scientific) for 30 min at 4 °C in binding buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10% glycerol, 0.5 mM EDTA, 1 mM 2-mercaptoethanol, 0.5% Nonidet P-40). .. The beads were washed with binding buffer three times, and then were incubated with the proteins for 1 h at 4 °C in binding buffer.

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  • 88
    Jena Bioscience bio atp
    dsDNA and CDN bind to the DEAD domain at the same sites. ( A ) Pull-down assays of DEAD, using bio-cGG in the presence of unlabeled <t>ISD</t> (left panel), and bio-ISD in the presence of unlabeled cGG (right panel). The final concentrations of unlabeled ISD or cGG are 0, 0.5, 1, 2 or 4 μM. ( B ) Pull-down assays of DEAD, using bio-ISD (left panel) or bio-cGG (right panel), in the presence of 1 mM unlabeled <t>ATP,</t> ADP or AMPPNP. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .
    Bio Atp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bio atp/product/Jena Bioscience
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bio atp - by Bioz Stars, 2021-05
    88/100 stars
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    dsDNA and CDN bind to the DEAD domain at the same sites. ( A ) Pull-down assays of DEAD, using bio-cGG in the presence of unlabeled ISD (left panel), and bio-ISD in the presence of unlabeled cGG (right panel). The final concentrations of unlabeled ISD or cGG are 0, 0.5, 1, 2 or 4 μM. ( B ) Pull-down assays of DEAD, using bio-ISD (left panel) or bio-cGG (right panel), in the presence of 1 mM unlabeled ATP, ADP or AMPPNP. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .

    Journal: Scientific Reports

    Article Title: Structural and Functional Analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide

    doi: 10.1038/srep34756

    Figure Lengend Snippet: dsDNA and CDN bind to the DEAD domain at the same sites. ( A ) Pull-down assays of DEAD, using bio-cGG in the presence of unlabeled ISD (left panel), and bio-ISD in the presence of unlabeled cGG (right panel). The final concentrations of unlabeled ISD or cGG are 0, 0.5, 1, 2 or 4 μM. ( B ) Pull-down assays of DEAD, using bio-ISD (left panel) or bio-cGG (right panel), in the presence of 1 mM unlabeled ATP, ADP or AMPPNP. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .

    Article Snippet: Bio-ISD, bio-cGG (2′-O- (6-[biotinyl]aminohexylcarbamoyl)-cyclic diguanosine monophosphate, B098-001, BioLog), bio-ATP (N6 -(6-amino)hexyl-adenosine-5′-triphosphate-biotin, NU-805-BIO, Jena Bioscience) and bio-AMPPNP (2′/3′-O-(2-aminoethyl-carbamoyl)-adenosine-5′-[(β,γ)-imido] triphosphate-biotin, NU-810-BIO, Jena Bioscience), each at a final concentration of 1 μM, were incubated with Dynabeads M-280 Streptavidin (Thermo Fisher Scientific) for 30 min at 4 °C in binding buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10% glycerol, 0.5 mM EDTA, 1 mM 2-mercaptoethanol, 0.5% Nonidet P-40).

    Techniques:

    Three forms of DDX41 reveal the structural rearrangement in the ATP-binding site. ( A ) Structure and sequence comparison between DDX41 and DDX3 (PDB ID: 5E7M). The Q motif and motif I of DDX3 are colored as in DDX41, whereas the other regions are colored silver. The amino-acid sequences of full-length DDX23 and DDX42 are the second and third most similar to that of DDX41. ( B ) Docking model of the DDX41 closed form bound to ATP (left panel), based on the DDX3-AMPPNP complex structure (PDB ID: 5E7M) (right panel). ( C ) Pull-down assays of the DEAD mutant, using bio-ATP and bio-AMPPNP. A cropped gel is shown. The full-length gel with the cropping lines indicated is shown in Figure S7 . ( D ) Docking models of the DDX41 open forms bound to ATP, based on the DDX3-AMPPNP complex structure (PDB ID: 5E7M). Models of the open form 1 (left panel) and the open form 2 (right panel) are shown.

    Journal: Scientific Reports

    Article Title: Structural and Functional Analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide

    doi: 10.1038/srep34756

    Figure Lengend Snippet: Three forms of DDX41 reveal the structural rearrangement in the ATP-binding site. ( A ) Structure and sequence comparison between DDX41 and DDX3 (PDB ID: 5E7M). The Q motif and motif I of DDX3 are colored as in DDX41, whereas the other regions are colored silver. The amino-acid sequences of full-length DDX23 and DDX42 are the second and third most similar to that of DDX41. ( B ) Docking model of the DDX41 closed form bound to ATP (left panel), based on the DDX3-AMPPNP complex structure (PDB ID: 5E7M) (right panel). ( C ) Pull-down assays of the DEAD mutant, using bio-ATP and bio-AMPPNP. A cropped gel is shown. The full-length gel with the cropping lines indicated is shown in Figure S7 . ( D ) Docking models of the DDX41 open forms bound to ATP, based on the DDX3-AMPPNP complex structure (PDB ID: 5E7M). Models of the open form 1 (left panel) and the open form 2 (right panel) are shown.

    Article Snippet: Bio-ISD, bio-cGG (2′-O- (6-[biotinyl]aminohexylcarbamoyl)-cyclic diguanosine monophosphate, B098-001, BioLog), bio-ATP (N6 -(6-amino)hexyl-adenosine-5′-triphosphate-biotin, NU-805-BIO, Jena Bioscience) and bio-AMPPNP (2′/3′-O-(2-aminoethyl-carbamoyl)-adenosine-5′-[(β,γ)-imido] triphosphate-biotin, NU-810-BIO, Jena Bioscience), each at a final concentration of 1 μM, were incubated with Dynabeads M-280 Streptavidin (Thermo Fisher Scientific) for 30 min at 4 °C in binding buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10% glycerol, 0.5 mM EDTA, 1 mM 2-mercaptoethanol, 0.5% Nonidet P-40).

    Techniques: Binding Assay, Sequencing, Mutagenesis

    The DDX41 DEAD domain binds to dsDNA and CDN. ( A ) FL-DDX41 and its truncated variants. DDX41 contains the DEAD domain (sky blue), the HELICc domain (orange) and the Zinc finger (ZF, gray). ( B ) Pull-down assays of DDX41, using bio-ISD (left panel) and bio-cGG (right panel). In all of the pull-down assays, the final concentration of bio-ISD, bio-cGG, bio-ATP or bio-AMPPNP is 1 μM, unless otherwise stated. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .

    Journal: Scientific Reports

    Article Title: Structural and Functional Analysis of DDX41: a bispecific immune receptor for DNA and cyclic dinucleotide

    doi: 10.1038/srep34756

    Figure Lengend Snippet: The DDX41 DEAD domain binds to dsDNA and CDN. ( A ) FL-DDX41 and its truncated variants. DDX41 contains the DEAD domain (sky blue), the HELICc domain (orange) and the Zinc finger (ZF, gray). ( B ) Pull-down assays of DDX41, using bio-ISD (left panel) and bio-cGG (right panel). In all of the pull-down assays, the final concentration of bio-ISD, bio-cGG, bio-ATP or bio-AMPPNP is 1 μM, unless otherwise stated. Gels were run under the same experimental conditions and are shown as cropped gels. Full-length gels with indicated cropping lines are shown in Figure S7 .

    Article Snippet: Bio-ISD, bio-cGG (2′-O- (6-[biotinyl]aminohexylcarbamoyl)-cyclic diguanosine monophosphate, B098-001, BioLog), bio-ATP (N6 -(6-amino)hexyl-adenosine-5′-triphosphate-biotin, NU-805-BIO, Jena Bioscience) and bio-AMPPNP (2′/3′-O-(2-aminoethyl-carbamoyl)-adenosine-5′-[(β,γ)-imido] triphosphate-biotin, NU-810-BIO, Jena Bioscience), each at a final concentration of 1 μM, were incubated with Dynabeads M-280 Streptavidin (Thermo Fisher Scientific) for 30 min at 4 °C in binding buffer (50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10% glycerol, 0.5 mM EDTA, 1 mM 2-mercaptoethanol, 0.5% Nonidet P-40).

    Techniques: Concentration Assay