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  • 97
    Thermo Fisher dgtp
    Dgtp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dgtp/product/Thermo Fisher
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    dgtp - by Bioz Stars, 2021-03
    97/100 stars
      Buy from Supplier

    99
    Thermo Fisher bigdye terminator cycle sequencing ready reaction kit
    Bigdye Terminator Cycle Sequencing Ready Reaction Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bigdye terminator cycle sequencing ready reaction kit/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bigdye terminator cycle sequencing ready reaction kit - by Bioz Stars, 2021-03
    99/100 stars
      Buy from Supplier

    93
    GE Healthcare dgtp
    Crystal structure of full-length <t>mSAMHD1</t> iso1 in complex with GTP and <t>dGTP</t> (2-Allo). a Surface representation of mSAMHD1 tetramer in three orthogonal views. Each subunit is shown in a different color (purple, orange, red, and green) with SAM domains highlighted. b Surface representation of the 2-Allo structure showing the allosteric binding pocket at the interface of three subunits (purple, red, and green). GTP and dGTP are shown with red sticks and the SAM-to-HD inter- and intra-subunit interactions are highlighted with selected interface residues shown in sticks. c Transparent surface representation of the SAM domain (lime green) capping the allosteric site
    Dgtp, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dgtp/product/GE Healthcare
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    dgtp - by Bioz Stars, 2021-03
    93/100 stars
      Buy from Supplier

    99
    PerkinElmer dgtp
    Crystal structure of full-length <t>mSAMHD1</t> iso1 in complex with GTP and <t>dGTP</t> (2-Allo). a Surface representation of mSAMHD1 tetramer in three orthogonal views. Each subunit is shown in a different color (purple, orange, red, and green) with SAM domains highlighted. b Surface representation of the 2-Allo structure showing the allosteric binding pocket at the interface of three subunits (purple, red, and green). GTP and dGTP are shown with red sticks and the SAM-to-HD inter- and intra-subunit interactions are highlighted with selected interface residues shown in sticks. c Transparent surface representation of the SAM domain (lime green) capping the allosteric site
    Dgtp, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dgtp/product/PerkinElmer
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    dgtp - by Bioz Stars, 2021-03
    99/100 stars
      Buy from Supplier


    N/A
    ADS BIOTEC dNTPs are packaged in 100 micromole quantities They can also be purchased where all four are premixed in 100 micromole quantities at 25 micromoles each
      Buy from Supplier

    Image Search Results


    Crystal structure of full-length mSAMHD1 iso1 in complex with GTP and dGTP (2-Allo). a Surface representation of mSAMHD1 tetramer in three orthogonal views. Each subunit is shown in a different color (purple, orange, red, and green) with SAM domains highlighted. b Surface representation of the 2-Allo structure showing the allosteric binding pocket at the interface of three subunits (purple, red, and green). GTP and dGTP are shown with red sticks and the SAM-to-HD inter- and intra-subunit interactions are highlighted with selected interface residues shown in sticks. c Transparent surface representation of the SAM domain (lime green) capping the allosteric site

    Journal: Nature Communications

    Article Title: The SAM domain of mouse SAMHD1 is critical for its activation and regulation

    doi: 10.1038/s41467-017-02783-8

    Figure Lengend Snippet: Crystal structure of full-length mSAMHD1 iso1 in complex with GTP and dGTP (2-Allo). a Surface representation of mSAMHD1 tetramer in three orthogonal views. Each subunit is shown in a different color (purple, orange, red, and green) with SAM domains highlighted. b Surface representation of the 2-Allo structure showing the allosteric binding pocket at the interface of three subunits (purple, red, and green). GTP and dGTP are shown with red sticks and the SAM-to-HD inter- and intra-subunit interactions are highlighted with selected interface residues shown in sticks. c Transparent surface representation of the SAM domain (lime green) capping the allosteric site

    Article Snippet: Analytical size-exclusion chromatography Purified samples of mSAMHD1 protein (2 mg/ml, 200 μl) mixed with dGTP or GTP (4 mM final concentration) were applied to a Superdex 200 10/300 GL column (GE Healthcare) pre-equilibrated in SAMHD1 buffer.

    Techniques: Binding Assay

    Crystal structures of mSAMHD1 activation intermediates. a Surface and ribbon representations of the mSAMHD1 structures at the allosteric site. Nucleotides are shown in red sticks and each subunit is colored uniquely. Left, No-Allo structure with no nucleotides bound. Middle, 1-Allo structure with dGTP bound to Allo-site 1. Right, 2-Allo structure with GTP and dGTP bound to Allo-site 1 and Allo-site 2, respectively. b , c Putty representation comparing the No-Allo and 1-Allo mSAMHD1 structures ( b ) and comparing the 1-Allo and 2-Allo structures ( c ) in two orthogonal views. The structures are aligned by superposition of dimer A. RMSD values are represented using the color spectrum and the thickness of the coil. d , e Surface representation of the No-Allo (left), 1-Allo (middle), and 2-Allo (right) structures showing conformational differences. Red triangles and arrows highlight the separation between a pair of SAM domains (green and purple). Cartoon schematics of the No-Allo (left) and 2-Allo structures (right) indicate the swinging (top row) and compacting (bottom row) motions of dimer A′ toward dimer A. Double-headed arrows highlight the distances between SAM domains as the tetramer becomes more compact

    Journal: Nature Communications

    Article Title: The SAM domain of mouse SAMHD1 is critical for its activation and regulation

    doi: 10.1038/s41467-017-02783-8

    Figure Lengend Snippet: Crystal structures of mSAMHD1 activation intermediates. a Surface and ribbon representations of the mSAMHD1 structures at the allosteric site. Nucleotides are shown in red sticks and each subunit is colored uniquely. Left, No-Allo structure with no nucleotides bound. Middle, 1-Allo structure with dGTP bound to Allo-site 1. Right, 2-Allo structure with GTP and dGTP bound to Allo-site 1 and Allo-site 2, respectively. b , c Putty representation comparing the No-Allo and 1-Allo mSAMHD1 structures ( b ) and comparing the 1-Allo and 2-Allo structures ( c ) in two orthogonal views. The structures are aligned by superposition of dimer A. RMSD values are represented using the color spectrum and the thickness of the coil. d , e Surface representation of the No-Allo (left), 1-Allo (middle), and 2-Allo (right) structures showing conformational differences. Red triangles and arrows highlight the separation between a pair of SAM domains (green and purple). Cartoon schematics of the No-Allo (left) and 2-Allo structures (right) indicate the swinging (top row) and compacting (bottom row) motions of dimer A′ toward dimer A. Double-headed arrows highlight the distances between SAM domains as the tetramer becomes more compact

    Article Snippet: Analytical size-exclusion chromatography Purified samples of mSAMHD1 protein (2 mg/ml, 200 μl) mixed with dGTP or GTP (4 mM final concentration) were applied to a Superdex 200 10/300 GL column (GE Healthcare) pre-equilibrated in SAMHD1 buffer.

    Techniques: Activation Assay

    The importance of SAM-to-HD interactions for mSAMHD1 oligomerization and activities. a , d Left, transparent surface representation of SAM-to-HD interface with important residues shown in sticks. Right, model of SAM-to-HD interface after mSAMHD1 residues are mutated to the corresponding hSAMHD1 residues. The red cross in a indicates a steric clash. b , e Left, SEC analysis of mSAMHD1 ( b ) or hSAMHD1 ( e ) variants before and after incubation with dGTP-α-S. Right, dNTPase assay for wild type and mutant mSAMHD1 proteins ( b ) or hSAMHD1 ( e ). Products were quantified by the malachite green assay. Each experiment was performed in triplicate. Error bars, s.d. c , f HIV-1 restriction by full-length mSAMHD1 iso1 ( c ) or hSAMHD1 ( f ) (WT and mutants) stably expressed in U937 cells after PMA differentiation. Immunoblotting (uncropped images in Supplementary Fig. 7 ) confirmed HA-tagged mSAMHD1 or hSAMHD1 expression. GAPDH was used as a loading control. Single-cycle HIV-1 infection of vector control cells was set as 100%. Each experiment was performed in triplicate. Error bars, s.d. *** p ≤ 0.0001

    Journal: Nature Communications

    Article Title: The SAM domain of mouse SAMHD1 is critical for its activation and regulation

    doi: 10.1038/s41467-017-02783-8

    Figure Lengend Snippet: The importance of SAM-to-HD interactions for mSAMHD1 oligomerization and activities. a , d Left, transparent surface representation of SAM-to-HD interface with important residues shown in sticks. Right, model of SAM-to-HD interface after mSAMHD1 residues are mutated to the corresponding hSAMHD1 residues. The red cross in a indicates a steric clash. b , e Left, SEC analysis of mSAMHD1 ( b ) or hSAMHD1 ( e ) variants before and after incubation with dGTP-α-S. Right, dNTPase assay for wild type and mutant mSAMHD1 proteins ( b ) or hSAMHD1 ( e ). Products were quantified by the malachite green assay. Each experiment was performed in triplicate. Error bars, s.d. c , f HIV-1 restriction by full-length mSAMHD1 iso1 ( c ) or hSAMHD1 ( f ) (WT and mutants) stably expressed in U937 cells after PMA differentiation. Immunoblotting (uncropped images in Supplementary Fig. 7 ) confirmed HA-tagged mSAMHD1 or hSAMHD1 expression. GAPDH was used as a loading control. Single-cycle HIV-1 infection of vector control cells was set as 100%. Each experiment was performed in triplicate. Error bars, s.d. *** p ≤ 0.0001

    Article Snippet: Analytical size-exclusion chromatography Purified samples of mSAMHD1 protein (2 mg/ml, 200 μl) mixed with dGTP or GTP (4 mM final concentration) were applied to a Superdex 200 10/300 GL column (GE Healthcare) pre-equilibrated in SAMHD1 buffer.

    Techniques: Size-exclusion Chromatography, Incubation, Mutagenesis, Malachite Green Assay, Stable Transfection, Expressing, Infection, Plasmid Preparation