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
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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
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Buy from Supplier |
GE Healthcare
dgtp ![]() 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
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PerkinElmer
dgtp ![]() 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 |
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
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Image Search Results

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
Techniques: Binding Assay

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
Techniques: Activation Assay

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