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Becton Dickinson mitochondrial atpase
Mitochondrial Atpase, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 85 stars, based on 1 article reviews
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mitochondrial atpase - by Bioz Stars, 2020-05
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Article Title: Toxicity of the Flame-Retardant BDE-49 on Brain Mitochondria and Neuronal Progenitor Striatal Cells Enhanced by a PTEN-Deficient Background
Article Snippet: Antinitrotyrosine antibody (clone 1A6) was from Millipore (Billerica, MA), and the antibody anti-β subunit of mitochondrial ATPase was from BD Biosciences (San Jose, CA).

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    Becton Dickinson atpases present
    Direction of metal transport by Cu+ <t>-ATPases</t>
    Atpases Present, supplied by Becton Dickinson, 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/atpases present/product/Becton Dickinson
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    atpases present - by Bioz Stars, 2020-05
    85/100 stars
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    Direction of metal transport by Cu+ -ATPases

    Journal: Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine

    Article Title: The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function

    doi: 10.1007/s10534-010-9404-3

    Figure Lengend Snippet: Direction of metal transport by Cu+ -ATPases

    Article Snippet: All Cu+ -ATPases present eight transmembrane segments where the transport metal binding sites are located (see below), and two major intracellular loops containing the actuator (A-domain) and the ATP-binding domains (ATP-BD) ( ) ( ; ; ).

    Techniques:

    Unrooted tree of Cu + ). Characterized Cu + - ATPases in this subgroup are indicated in blue ( R. capsulatus CcoI, B. japonicum FixI, S. meliloti FixI, R. gelatinosus CtpA, P. aeruginosa

    Journal: Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine

    Article Title: The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function

    doi: 10.1007/s10534-010-9404-3

    Figure Lengend Snippet: Unrooted tree of Cu + ). Characterized Cu + - ATPases in this subgroup are indicated in blue ( R. capsulatus CcoI, B. japonicum FixI, S. meliloti FixI, R. gelatinosus CtpA, P. aeruginosa

    Article Snippet: All Cu+ -ATPases present eight transmembrane segments where the transport metal binding sites are located (see below), and two major intracellular loops containing the actuator (A-domain) and the ATP-binding domains (ATP-BD) ( ) ( ; ; ).

    Techniques: