n 6 benzyl atpγs  (Jena Bioscience)


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    Name:
    ATPγS
    Description:

    Catalog Number:
    nu-406-25
    Price:
    202.45
    Applications:
    Modulation of intracellular signalling[1,2] Signalling of purinergic receptors[3] Regulation of cation channels[4] Modulation of cytokine secretion[5] Substrate for kinases[6] 5' end labeling with T4 Polynucleotide Kinase (T4 PNK) of DNA[9] and RNA[9,10] Agonistic ligand, mainly for nucleoside receptor A1 Nucleosidephosphates stabilized against hydrolytic degradation can directly bind to nucleoside receptors.
    Purity:
    ≥ 90 % (HPLC), contains < 10 % ADP
    Category:
    Nucleotides Nucleosides
    Buy from Supplier


    Structured Review

    Jena Bioscience n 6 benzyl atpγs
    Phot1 containing a modified gatekeeper residue (T740G) can accommodate <t>N</t> 6 <t>-benzyl-ATPγS</t> and undergo thiophosphorylation in vitro . A , immunoblot of a kinase assay containing cell-free expressed wildtype phot1, phot1-D806N, or phot1-T740G in the presence of N 6 -benzyl-ATPγS. Reactions were carried out in the absence ( D ) or presence of 20 s of white light ( L ), and thiophosphorylation was detected using anti-thiophosphoester antibody (α -thioP ). An immunoblot analysis of phot1 protein levels using anti-HA antibody is shown below. B , phot1-T740G thiophosphorylation in the presence of the kinase inhibitor 1-NM-PP1 or DMSO as a control. Ponceau staining of cell-free expression reactions is shown below to indicate equal protein loading.

    https://www.bioz.com/result/n 6 benzyl atpγs/product/Jena Bioscience
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    n 6 benzyl atpγs - by Bioz Stars, 2020-07
    93/100 stars

    Images

    1) Product Images from "A chemical genetic approach to engineer phototropin kinases for substrate labeling"

    Article Title: A chemical genetic approach to engineer phototropin kinases for substrate labeling

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA118.001834

    Phot1 containing a modified gatekeeper residue (T740G) can accommodate N 6 -benzyl-ATPγS and undergo thiophosphorylation in vitro . A , immunoblot of a kinase assay containing cell-free expressed wildtype phot1, phot1-D806N, or phot1-T740G in the presence of N 6 -benzyl-ATPγS. Reactions were carried out in the absence ( D ) or presence of 20 s of white light ( L ), and thiophosphorylation was detected using anti-thiophosphoester antibody (α -thioP ). An immunoblot analysis of phot1 protein levels using anti-HA antibody is shown below. B , phot1-T740G thiophosphorylation in the presence of the kinase inhibitor 1-NM-PP1 or DMSO as a control. Ponceau staining of cell-free expression reactions is shown below to indicate equal protein loading.
    Figure Legend Snippet: Phot1 containing a modified gatekeeper residue (T740G) can accommodate N 6 -benzyl-ATPγS and undergo thiophosphorylation in vitro . A , immunoblot of a kinase assay containing cell-free expressed wildtype phot1, phot1-D806N, or phot1-T740G in the presence of N 6 -benzyl-ATPγS. Reactions were carried out in the absence ( D ) or presence of 20 s of white light ( L ), and thiophosphorylation was detected using anti-thiophosphoester antibody (α -thioP ). An immunoblot analysis of phot1 protein levels using anti-HA antibody is shown below. B , phot1-T740G thiophosphorylation in the presence of the kinase inhibitor 1-NM-PP1 or DMSO as a control. Ponceau staining of cell-free expression reactions is shown below to indicate equal protein loading.

    Techniques Used: Modification, In Vitro, Kinase Assay, Staining, Expressing

    2) Product Images from "CryoEM structures of human CMG - ATPγS - DNA and CMG - AND-1 complexes"

    Article Title: CryoEM structures of human CMG - ATPγS - DNA and CMG - AND-1 complexes

    Journal: bioRxiv

    doi: 10.1101/2020.01.22.914192

    Protein-DNA interactions in the human CMG-ATPγS-DNA complex. MCM chains are coloured coded as in Figure 1 . A Side view of the CMG-ATPγS-DNA complex, highlighting the position of ssDNA within the MCM C-tier. The MCM subunits are shown as transparent molecular surfaces and the DNA is drawn as a dark grey ribbon. Cdc45 and GINS have been omitted for clarity. B Schematic drawing illustrating the DNA footprint and ATP status of each MCM subunit. C The staircase configuration of the H2I and PS1 DNA-binding loops around the ssDNA spiral, from MCM2 (pink) at the top (5′-end of the DNA) to MCM5 (yellow) at the bottom (3′-end).
    Figure Legend Snippet: Protein-DNA interactions in the human CMG-ATPγS-DNA complex. MCM chains are coloured coded as in Figure 1 . A Side view of the CMG-ATPγS-DNA complex, highlighting the position of ssDNA within the MCM C-tier. The MCM subunits are shown as transparent molecular surfaces and the DNA is drawn as a dark grey ribbon. Cdc45 and GINS have been omitted for clarity. B Schematic drawing illustrating the DNA footprint and ATP status of each MCM subunit. C The staircase configuration of the H2I and PS1 DNA-binding loops around the ssDNA spiral, from MCM2 (pink) at the top (5′-end of the DNA) to MCM5 (yellow) at the bottom (3′-end).

    Techniques Used: Binding Assay

    Conformational coupling of ATP status and DNA-binding loops. A Spacefill representation of the MCM C-tier, colour-coded according to ATP status. B Ribbon representation of MCM4 and DNA, showing the reciprocal position of the ATPγS moiety and the H2I and PS1 DNA-binding loops. C Superposition of MCM ATPase domains, highlighting the relative position of their DNA-binding loops (MCM2 is omitted, see Supplementary figure 11). The H2I α N helix of MCM5 is disordered and drawn as a dotted line. The MCM ATPase domains are coloured according to ATP status, as in panel A.
    Figure Legend Snippet: Conformational coupling of ATP status and DNA-binding loops. A Spacefill representation of the MCM C-tier, colour-coded according to ATP status. B Ribbon representation of MCM4 and DNA, showing the reciprocal position of the ATPγS moiety and the H2I and PS1 DNA-binding loops. C Superposition of MCM ATPase domains, highlighting the relative position of their DNA-binding loops (MCM2 is omitted, see Supplementary figure 11). The H2I α N helix of MCM5 is disordered and drawn as a dotted line. The MCM ATPase domains are coloured according to ATP status, as in panel A.

    Techniques Used: Binding Assay

    ATPγS binding in the CMG-ATPγS-DNA complex. In the middle-right panel, the MCM C-tier is shown in molecular surface representation, clipped from the N-tier end, to reveal the nucleotide bound at each MCM interface. The cartoon drawing above the panel recapitulates the ATP status of MCM2-7 (AGS stands for ATPγS). Details of nucleotide binding are provided in the oval panels for each of the five nucleotide-bound interfaces. MCM chains are colour-coded as in Figure 1 .
    Figure Legend Snippet: ATPγS binding in the CMG-ATPγS-DNA complex. In the middle-right panel, the MCM C-tier is shown in molecular surface representation, clipped from the N-tier end, to reveal the nucleotide bound at each MCM interface. The cartoon drawing above the panel recapitulates the ATP status of MCM2-7 (AGS stands for ATPγS). Details of nucleotide binding are provided in the oval panels for each of the five nucleotide-bound interfaces. MCM chains are colour-coded as in Figure 1 .

    Techniques Used: Binding Assay

    Structure of the human CMG-ATPγS-DNA DNA helicase. A 3.3Å cryoEM map of CMG-ATPγS-DNA. MCM2-7 are coloured according to chain: MCM2 is pink, MCM3 cyan, MCM4 green, MCM5 yellow, MCM6 orange and MCM7 blue, following the colour scheme of Eickhoff and colleagues ( Eickhoff et al., 2019 ). The DNA is coloured white, and the Cdc45 and GINS grey. B Top and side views of a ribbon model of the atomic structure of CMG-ATPγS-DNA. The N- and C-tier of the CMG are highlighted in the side view, as well as the location of MCM2 and MCM6’s C-terminal WH domains. Colouring as in panel A.
    Figure Legend Snippet: Structure of the human CMG-ATPγS-DNA DNA helicase. A 3.3Å cryoEM map of CMG-ATPγS-DNA. MCM2-7 are coloured according to chain: MCM2 is pink, MCM3 cyan, MCM4 green, MCM5 yellow, MCM6 orange and MCM7 blue, following the colour scheme of Eickhoff and colleagues ( Eickhoff et al., 2019 ). The DNA is coloured white, and the Cdc45 and GINS grey. B Top and side views of a ribbon model of the atomic structure of CMG-ATPγS-DNA. The N- and C-tier of the CMG are highlighted in the side view, as well as the location of MCM2 and MCM6’s C-terminal WH domains. Colouring as in panel A.

    Techniques Used:

    Related Articles

    other:

    Article Title: Connexin-43-dependent ATP release mediates macrophage activation during sepsis
    Article Snippet: The following purinergic agonists and antagonists were used: ATPgammaS (Jena Bioscience, # NU-406–50), apyrase (Sigma-Aldrich, # A6132), suramin (non-selective P2 antagonist, Tocris, # 1472); NF110 (P2 × 3 antagonist, Tocris, # 2548); 5BDBD (P2 × 4 antagonist, Tocris, # 3579); A804598 (P2 × 7 antagonist, Tocris, # 4473); MRS2500 and MRS2279 (P2Y1 antagonist, Tocris, # 2159 and # 2158); AR-C 118925XX (P2Y2 antagonist, Tocris, # 4890); MRS2578 (P2Y6 antagonist, Tocris, # 2146); NF157 (P2Y11/P2 × 1 antagonist, Tocris, # 2450).

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  • 93
    Jena Bioscience n 6 benzyl atpγs
    Phot1 containing a modified gatekeeper residue (T740G) can accommodate <t>N</t> 6 <t>-benzyl-ATPγS</t> and undergo thiophosphorylation in vitro . A , immunoblot of a kinase assay containing cell-free expressed wildtype phot1, phot1-D806N, or phot1-T740G in the presence of N 6 -benzyl-ATPγS. Reactions were carried out in the absence ( D ) or presence of 20 s of white light ( L ), and thiophosphorylation was detected using anti-thiophosphoester antibody (α -thioP ). An immunoblot analysis of phot1 protein levels using anti-HA antibody is shown below. B , phot1-T740G thiophosphorylation in the presence of the kinase inhibitor 1-NM-PP1 or DMSO as a control. Ponceau staining of cell-free expression reactions is shown below to indicate equal protein loading.
    N 6 Benzyl Atpγs, supplied by Jena Bioscience, 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/n 6 benzyl atpγs/product/Jena Bioscience
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    n 6 benzyl atpγs - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    Image Search Results


    Phot1 containing a modified gatekeeper residue (T740G) can accommodate N 6 -benzyl-ATPγS and undergo thiophosphorylation in vitro . A , immunoblot of a kinase assay containing cell-free expressed wildtype phot1, phot1-D806N, or phot1-T740G in the presence of N 6 -benzyl-ATPγS. Reactions were carried out in the absence ( D ) or presence of 20 s of white light ( L ), and thiophosphorylation was detected using anti-thiophosphoester antibody (α -thioP ). An immunoblot analysis of phot1 protein levels using anti-HA antibody is shown below. B , phot1-T740G thiophosphorylation in the presence of the kinase inhibitor 1-NM-PP1 or DMSO as a control. Ponceau staining of cell-free expression reactions is shown below to indicate equal protein loading.

    Journal: The Journal of Biological Chemistry

    Article Title: A chemical genetic approach to engineer phototropin kinases for substrate labeling

    doi: 10.1074/jbc.RA118.001834

    Figure Lengend Snippet: Phot1 containing a modified gatekeeper residue (T740G) can accommodate N 6 -benzyl-ATPγS and undergo thiophosphorylation in vitro . A , immunoblot of a kinase assay containing cell-free expressed wildtype phot1, phot1-D806N, or phot1-T740G in the presence of N 6 -benzyl-ATPγS. Reactions were carried out in the absence ( D ) or presence of 20 s of white light ( L ), and thiophosphorylation was detected using anti-thiophosphoester antibody (α -thioP ). An immunoblot analysis of phot1 protein levels using anti-HA antibody is shown below. B , phot1-T740G thiophosphorylation in the presence of the kinase inhibitor 1-NM-PP1 or DMSO as a control. Ponceau staining of cell-free expression reactions is shown below to indicate equal protein loading.

    Article Snippet: N 6 -benzyl-ATPγS (Jena Bioscience) was used at a final concentration of 100 μ m for phot1 autophosphorylation or 500 μ m for substrate phosphorylation and for phosphorylation screening with plant protein extracts.

    Techniques: Modification, In Vitro, Kinase Assay, Staining, Expressing

    Protein-DNA interactions in the human CMG-ATPγS-DNA complex. MCM chains are coloured coded as in Figure 1 . A Side view of the CMG-ATPγS-DNA complex, highlighting the position of ssDNA within the MCM C-tier. The MCM subunits are shown as transparent molecular surfaces and the DNA is drawn as a dark grey ribbon. Cdc45 and GINS have been omitted for clarity. B Schematic drawing illustrating the DNA footprint and ATP status of each MCM subunit. C The staircase configuration of the H2I and PS1 DNA-binding loops around the ssDNA spiral, from MCM2 (pink) at the top (5′-end of the DNA) to MCM5 (yellow) at the bottom (3′-end).

    Journal: bioRxiv

    Article Title: CryoEM structures of human CMG - ATPγS - DNA and CMG - AND-1 complexes

    doi: 10.1101/2020.01.22.914192

    Figure Lengend Snippet: Protein-DNA interactions in the human CMG-ATPγS-DNA complex. MCM chains are coloured coded as in Figure 1 . A Side view of the CMG-ATPγS-DNA complex, highlighting the position of ssDNA within the MCM C-tier. The MCM subunits are shown as transparent molecular surfaces and the DNA is drawn as a dark grey ribbon. Cdc45 and GINS have been omitted for clarity. B Schematic drawing illustrating the DNA footprint and ATP status of each MCM subunit. C The staircase configuration of the H2I and PS1 DNA-binding loops around the ssDNA spiral, from MCM2 (pink) at the top (5′-end of the DNA) to MCM5 (yellow) at the bottom (3′-end).

    Article Snippet: After sample loading, the column was washed for 5 column volumes using Buffer N with 2 mM DTT, followed by 5 column volumes of Buffer S. To form the CMG-DNA complex, ∼900 μL of 4 μM forked DNA duplex and 100 μM ATPγS (Jena Bioscience, #NU-406-50) in Buffer S was applied to the column at 0.05 mL/min.

    Techniques: Binding Assay

    Conformational coupling of ATP status and DNA-binding loops. A Spacefill representation of the MCM C-tier, colour-coded according to ATP status. B Ribbon representation of MCM4 and DNA, showing the reciprocal position of the ATPγS moiety and the H2I and PS1 DNA-binding loops. C Superposition of MCM ATPase domains, highlighting the relative position of their DNA-binding loops (MCM2 is omitted, see Supplementary figure 11). The H2I α N helix of MCM5 is disordered and drawn as a dotted line. The MCM ATPase domains are coloured according to ATP status, as in panel A.

    Journal: bioRxiv

    Article Title: CryoEM structures of human CMG - ATPγS - DNA and CMG - AND-1 complexes

    doi: 10.1101/2020.01.22.914192

    Figure Lengend Snippet: Conformational coupling of ATP status and DNA-binding loops. A Spacefill representation of the MCM C-tier, colour-coded according to ATP status. B Ribbon representation of MCM4 and DNA, showing the reciprocal position of the ATPγS moiety and the H2I and PS1 DNA-binding loops. C Superposition of MCM ATPase domains, highlighting the relative position of their DNA-binding loops (MCM2 is omitted, see Supplementary figure 11). The H2I α N helix of MCM5 is disordered and drawn as a dotted line. The MCM ATPase domains are coloured according to ATP status, as in panel A.

    Article Snippet: After sample loading, the column was washed for 5 column volumes using Buffer N with 2 mM DTT, followed by 5 column volumes of Buffer S. To form the CMG-DNA complex, ∼900 μL of 4 μM forked DNA duplex and 100 μM ATPγS (Jena Bioscience, #NU-406-50) in Buffer S was applied to the column at 0.05 mL/min.

    Techniques: Binding Assay

    ATPγS binding in the CMG-ATPγS-DNA complex. In the middle-right panel, the MCM C-tier is shown in molecular surface representation, clipped from the N-tier end, to reveal the nucleotide bound at each MCM interface. The cartoon drawing above the panel recapitulates the ATP status of MCM2-7 (AGS stands for ATPγS). Details of nucleotide binding are provided in the oval panels for each of the five nucleotide-bound interfaces. MCM chains are colour-coded as in Figure 1 .

    Journal: bioRxiv

    Article Title: CryoEM structures of human CMG - ATPγS - DNA and CMG - AND-1 complexes

    doi: 10.1101/2020.01.22.914192

    Figure Lengend Snippet: ATPγS binding in the CMG-ATPγS-DNA complex. In the middle-right panel, the MCM C-tier is shown in molecular surface representation, clipped from the N-tier end, to reveal the nucleotide bound at each MCM interface. The cartoon drawing above the panel recapitulates the ATP status of MCM2-7 (AGS stands for ATPγS). Details of nucleotide binding are provided in the oval panels for each of the five nucleotide-bound interfaces. MCM chains are colour-coded as in Figure 1 .

    Article Snippet: After sample loading, the column was washed for 5 column volumes using Buffer N with 2 mM DTT, followed by 5 column volumes of Buffer S. To form the CMG-DNA complex, ∼900 μL of 4 μM forked DNA duplex and 100 μM ATPγS (Jena Bioscience, #NU-406-50) in Buffer S was applied to the column at 0.05 mL/min.

    Techniques: Binding Assay

    Structure of the human CMG-ATPγS-DNA DNA helicase. A 3.3Å cryoEM map of CMG-ATPγS-DNA. MCM2-7 are coloured according to chain: MCM2 is pink, MCM3 cyan, MCM4 green, MCM5 yellow, MCM6 orange and MCM7 blue, following the colour scheme of Eickhoff and colleagues ( Eickhoff et al., 2019 ). The DNA is coloured white, and the Cdc45 and GINS grey. B Top and side views of a ribbon model of the atomic structure of CMG-ATPγS-DNA. The N- and C-tier of the CMG are highlighted in the side view, as well as the location of MCM2 and MCM6’s C-terminal WH domains. Colouring as in panel A.

    Journal: bioRxiv

    Article Title: CryoEM structures of human CMG - ATPγS - DNA and CMG - AND-1 complexes

    doi: 10.1101/2020.01.22.914192

    Figure Lengend Snippet: Structure of the human CMG-ATPγS-DNA DNA helicase. A 3.3Å cryoEM map of CMG-ATPγS-DNA. MCM2-7 are coloured according to chain: MCM2 is pink, MCM3 cyan, MCM4 green, MCM5 yellow, MCM6 orange and MCM7 blue, following the colour scheme of Eickhoff and colleagues ( Eickhoff et al., 2019 ). The DNA is coloured white, and the Cdc45 and GINS grey. B Top and side views of a ribbon model of the atomic structure of CMG-ATPγS-DNA. The N- and C-tier of the CMG are highlighted in the side view, as well as the location of MCM2 and MCM6’s C-terminal WH domains. Colouring as in panel A.

    Article Snippet: After sample loading, the column was washed for 5 column volumes using Buffer N with 2 mM DTT, followed by 5 column volumes of Buffer S. To form the CMG-DNA complex, ∼900 μL of 4 μM forked DNA duplex and 100 μM ATPγS (Jena Bioscience, #NU-406-50) in Buffer S was applied to the column at 0.05 mL/min.

    Techniques: