ω conotoxin mviia  (Alomone Labs)


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    Structured Review

    Alomone Labs ω conotoxin mviia
    ω Conotoxin Mviia, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ω conotoxin mviia/product/Alomone Labs
    Average 85 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    ω conotoxin mviia - by Bioz Stars, 2022-09
    85/100 stars

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    Alomone Labs ziconotide
    Structure and stability of Hm1a. ( A ) Primary structures of Hm1a and Hm1b. Nonconserved residues are highlighted in blue. The disulfide-bond architecture is illustrated above the sequences. ( B ) 3D structure of Hm1a. Disulfide bonds are shown in red, β strands are green, and the N- and C-termini are labeled. ( C ) Cystine knot motif in Hm1a. The C15–C28 disulfide bond (orange) bisects a closed loop formed by the other two disulfide bonds (red) and the intervening sections of peptide backbone (gray). ( D ) Surface representation of Hm1a showing exposed hydrophobic residues that are conserved in Hm1b (green) and residues that differ between Hm1a and Hm1b (blue). ( E ) Speculative model for interaction of the hydrophobic face of Hm1a with the DIV voltage sensor of Na V 1.1. ( F ) Stability of Hm1a, hANP, and <t>ziconotide</t> in human CSF.
    Ziconotide, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ziconotide/product/Alomone Labs
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ziconotide - by Bioz Stars, 2022-09
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    90
    Alomone Labs n type ca2 channel blocker conotoxin mviia
    Structure and stability of Hm1a. ( A ) Primary structures of Hm1a and Hm1b. Nonconserved residues are highlighted in blue. The disulfide-bond architecture is illustrated above the sequences. ( B ) 3D structure of Hm1a. Disulfide bonds are shown in red, β strands are green, and the N- and C-termini are labeled. ( C ) Cystine knot motif in Hm1a. The C15–C28 disulfide bond (orange) bisects a closed loop formed by the other two disulfide bonds (red) and the intervening sections of peptide backbone (gray). ( D ) Surface representation of Hm1a showing exposed hydrophobic residues that are conserved in Hm1b (green) and residues that differ between Hm1a and Hm1b (blue). ( E ) Speculative model for interaction of the hydrophobic face of Hm1a with the DIV voltage sensor of Na V 1.1. ( F ) Stability of Hm1a, hANP, and <t>ziconotide</t> in human CSF.
    N Type Ca2 Channel Blocker Conotoxin Mviia, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/n type ca2 channel blocker conotoxin mviia/product/Alomone Labs
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    n type ca2 channel blocker conotoxin mviia - by Bioz Stars, 2022-09
    90/100 stars
      Buy from Supplier

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    Structure and stability of Hm1a. ( A ) Primary structures of Hm1a and Hm1b. Nonconserved residues are highlighted in blue. The disulfide-bond architecture is illustrated above the sequences. ( B ) 3D structure of Hm1a. Disulfide bonds are shown in red, β strands are green, and the N- and C-termini are labeled. ( C ) Cystine knot motif in Hm1a. The C15–C28 disulfide bond (orange) bisects a closed loop formed by the other two disulfide bonds (red) and the intervening sections of peptide backbone (gray). ( D ) Surface representation of Hm1a showing exposed hydrophobic residues that are conserved in Hm1b (green) and residues that differ between Hm1a and Hm1b (blue). ( E ) Speculative model for interaction of the hydrophobic face of Hm1a with the DIV voltage sensor of Na V 1.1. ( F ) Stability of Hm1a, hANP, and ziconotide in human CSF.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Selective NaV1.1 activation rescues Dravet syndrome mice from seizures and premature death

    doi: 10.1073/pnas.1804764115

    Figure Lengend Snippet: Structure and stability of Hm1a. ( A ) Primary structures of Hm1a and Hm1b. Nonconserved residues are highlighted in blue. The disulfide-bond architecture is illustrated above the sequences. ( B ) 3D structure of Hm1a. Disulfide bonds are shown in red, β strands are green, and the N- and C-termini are labeled. ( C ) Cystine knot motif in Hm1a. The C15–C28 disulfide bond (orange) bisects a closed loop formed by the other two disulfide bonds (red) and the intervening sections of peptide backbone (gray). ( D ) Surface representation of Hm1a showing exposed hydrophobic residues that are conserved in Hm1b (green) and residues that differ between Hm1a and Hm1b (blue). ( E ) Speculative model for interaction of the hydrophobic face of Hm1a with the DIV voltage sensor of Na V 1.1. ( F ) Stability of Hm1a, hANP, and ziconotide in human CSF.

    Article Snippet: The supernatant (10 μL) was then processed [150 mm × 2.1 mm; flow rate 0.2 mL/min; gradient of 2–40% solvent B (90% acetonitrile, 0.1% FA) in solvent A (0.1% FA) over 14 min] coupled to a TripleTOF 5600 mass spectrometer (AB SCIEX) with a cycle time of 0.2751 s. Peak areas were measured for triple-, quadruple-, and quintuple-charge states and were analyzed using PeakView and MultiQuant (Sciex) software. hANP (1 μM; GenScript) and ziconotide (ω-conotoxin MVIIA, 1 μM; Alomone Labs) served as controls.

    Techniques: Labeling

    Structure and stability of Hm1a. ( A ) Primary structures of Hm1a and Hm1b. Nonconserved residues are highlighted in blue. The disulfide-bond architecture is illustrated above the sequences. ( B ) 3D structure of Hm1a. Disulfide bonds are shown in red, β strands are green, and the N- and C-termini are labeled. ( C ) Cystine knot motif in Hm1a. The C15–C28 disulfide bond (orange) bisects a closed loop formed by the other two disulfide bonds (red) and the intervening sections of peptide backbone (gray). ( D ) Surface representation of Hm1a showing exposed hydrophobic residues that are conserved in Hm1b (green) and residues that differ between Hm1a and Hm1b (blue). ( E ) Speculative model for interaction of the hydrophobic face of Hm1a with the DIV voltage sensor of Na V 1.1. ( F ) Stability of Hm1a, hANP, and ziconotide in human CSF.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Selective NaV1.1 activation rescues Dravet syndrome mice from seizures and premature death

    doi: 10.1073/pnas.1804764115

    Figure Lengend Snippet: Structure and stability of Hm1a. ( A ) Primary structures of Hm1a and Hm1b. Nonconserved residues are highlighted in blue. The disulfide-bond architecture is illustrated above the sequences. ( B ) 3D structure of Hm1a. Disulfide bonds are shown in red, β strands are green, and the N- and C-termini are labeled. ( C ) Cystine knot motif in Hm1a. The C15–C28 disulfide bond (orange) bisects a closed loop formed by the other two disulfide bonds (red) and the intervening sections of peptide backbone (gray). ( D ) Surface representation of Hm1a showing exposed hydrophobic residues that are conserved in Hm1b (green) and residues that differ between Hm1a and Hm1b (blue). ( E ) Speculative model for interaction of the hydrophobic face of Hm1a with the DIV voltage sensor of Na V 1.1. ( F ) Stability of Hm1a, hANP, and ziconotide in human CSF.

    Article Snippet: The supernatant (10 μL) was then processed [150 mm × 2.1 mm; flow rate 0.2 mL/min; gradient of 2–40% solvent B (90% acetonitrile, 0.1% FA) in solvent A (0.1% FA) over 14 min] coupled to a TripleTOF 5600 mass spectrometer (AB SCIEX) with a cycle time of 0.2751 s. Peak areas were measured for triple-, quadruple-, and quintuple-charge states and were analyzed using PeakView and MultiQuant (Sciex) software. hANP (1 μM; GenScript) and ziconotide (ω-conotoxin MVIIA, 1 μM; Alomone Labs) served as controls.

    Techniques: Labeling