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mgh 24 a0a0d7lw76  (ATCC)


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    Structured Review

    ATCC mgh 24 a0a0d7lw76
    Mgh 24 A0a0d7lw76, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/64690/Kuzuhaea+moniliformis+Benjamin/pmc11419355__ppat__1012534__s001-8-99-137
    Average 93 stars, based on 2 article reviews
    mgh 24 a0a0d7lw76 - by Bioz Stars, 2026-09
    93/100 stars

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    Related Articles

    Cloning:

    Article Title: Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors
    Article Snippet: .. Cloning, expression, and folding of the catalytic domain of MT1-MMP The coding sequence of the catalytic domain of human MMP-14 (104–308) was amplified from MGC clone 64,690 (ATCC; GenBank accession number: {"type":"entrez-nucleotide","attrs":{"text":"BC064803","term_id":"40675474","term_text":"BC064803"}} BC064803 ) using the primers: 5′-CGAAGGAAGCGCCATATGATCCAGGGTCTCAAATGGCAACATAAT-3′ (forward; incorporates a Nde I site and an initiating methionine) and 5′-GGTGTCAAAGTT GGATCC TCA GATGTTGGGCCCATAGGTGGGGTT-3′ (reverse; incorporates a stop codon and a BamH 1 site). ..

    Expressing:

    Article Title: Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors
    Article Snippet: .. Cloning, expression, and folding of the catalytic domain of MT1-MMP The coding sequence of the catalytic domain of human MMP-14 (104–308) was amplified from MGC clone 64,690 (ATCC; GenBank accession number: {"type":"entrez-nucleotide","attrs":{"text":"BC064803","term_id":"40675474","term_text":"BC064803"}} BC064803 ) using the primers: 5′-CGAAGGAAGCGCCATATGATCCAGGGTCTCAAATGGCAACATAAT-3′ (forward; incorporates a Nde I site and an initiating methionine) and 5′-GGTGTCAAAGTT GGATCC TCA GATGTTGGGCCCATAGGTGGGGTT-3′ (reverse; incorporates a stop codon and a BamH 1 site). ..

    Sequencing:

    Article Title: Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors
    Article Snippet: .. Cloning, expression, and folding of the catalytic domain of MT1-MMP The coding sequence of the catalytic domain of human MMP-14 (104–308) was amplified from MGC clone 64,690 (ATCC; GenBank accession number: {"type":"entrez-nucleotide","attrs":{"text":"BC064803","term_id":"40675474","term_text":"BC064803"}} BC064803 ) using the primers: 5′-CGAAGGAAGCGCCATATGATCCAGGGTCTCAAATGGCAACATAAT-3′ (forward; incorporates a Nde I site and an initiating methionine) and 5′-GGTGTCAAAGTT GGATCC TCA GATGTTGGGCCCATAGGTGGGGTT-3′ (reverse; incorporates a stop codon and a BamH 1 site). ..

    Amplification:

    Article Title: Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors
    Article Snippet: .. Cloning, expression, and folding of the catalytic domain of MT1-MMP The coding sequence of the catalytic domain of human MMP-14 (104–308) was amplified from MGC clone 64,690 (ATCC; GenBank accession number: {"type":"entrez-nucleotide","attrs":{"text":"BC064803","term_id":"40675474","term_text":"BC064803"}} BC064803 ) using the primers: 5′-CGAAGGAAGCGCCATATGATCCAGGGTCTCAAATGGCAACATAAT-3′ (forward; incorporates a Nde I site and an initiating methionine) and 5′-GGTGTCAAAGTT GGATCC TCA GATGTTGGGCCCATAGGTGGGGTT-3′ (reverse; incorporates a stop codon and a BamH 1 site). ..

    Concentration Assay:

    Article Title: Rapid method for screening enoate reductase activity in yeasts.
    Article Snippet: Contents lists available at ScienceDirect Journal of Microbiological Methods j ourna l homepage: www.e lsev ie r.com/ locate / jmicmeth Review Rapid method for screening enoate reductase activity in yeasts Stefano Raimondi a, Lucia Roncaglia a, Alberto Amaretti a, Alan Leonardi a, Pietro Buzzini b, Luca Forti a, Maddalena Rossi a,⁎ a Department of Chemistry, University of Modena and Reggio Emilia, Modena, Italy b Department of Applied Biology and Industrial Yeasts Collection DBVPG, University of Perugia, Perugia, Italy ⁎ Corresponding author.. Department of Chemistry, Un Emilia, Via Campi183, 41125Modena, Italy.. Tel.



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