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dn c-src mutant  (Upstate Biotechnology Inc)

 
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    Structured Review

    Upstate Biotechnology Inc dn c-src mutant
    Dn C Src Mutant, supplied by Upstate Biotechnology Inc, 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/product/c-src+dn/dn+c+src+mutant/pm15208664-210-0-49
    Average 90 stars, based on 1 article reviews
    dn c-src mutant - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Mutagenesis:

    Article Title: Involvement of c-Src kinase in the regulation of TGF-beta1-induced apoptosis.
    Article Snippet: DN c-Src mutant has two mutations, an arginine for lysine substitution (K296R) in the ATP binding pocket of the tyrosine kinase domain that abolishes phosphotransferase activity, and a phenylalanine for tyrosine substitution (Y528F) that abolishes phosphorylation, thereby preventing intramolecular interaction between the C-terminus and the SH2 domain of c-Src (Upstate Biotechnology, Lake Placid, NY, USA).

    Binding Assay:

    Article Title: Involvement of c-Src kinase in the regulation of TGF-beta1-induced apoptosis.
    Article Snippet: DN c-Src mutant has two mutations, an arginine for lysine substitution (K296R) in the ATP binding pocket of the tyrosine kinase domain that abolishes phosphotransferase activity, and a phenylalanine for tyrosine substitution (Y528F) that abolishes phosphorylation, thereby preventing intramolecular interaction between the C-terminus and the SH2 domain of c-Src (Upstate Biotechnology, Lake Placid, NY, USA).

    Activity Assay:

    Article Title: Involvement of c-Src kinase in the regulation of TGF-beta1-induced apoptosis.
    Article Snippet: DN c-Src mutant has two mutations, an arginine for lysine substitution (K296R) in the ATP binding pocket of the tyrosine kinase domain that abolishes phosphotransferase activity, and a phenylalanine for tyrosine substitution (Y528F) that abolishes phosphorylation, thereby preventing intramolecular interaction between the C-terminus and the SH2 domain of c-Src (Upstate Biotechnology, Lake Placid, NY, USA).

    Phospho-proteomics:

    Article Title: Involvement of c-Src kinase in the regulation of TGF-beta1-induced apoptosis.
    Article Snippet: DN c-Src mutant has two mutations, an arginine for lysine substitution (K296R) in the ATP binding pocket of the tyrosine kinase domain that abolishes phosphotransferase activity, and a phenylalanine for tyrosine substitution (Y528F) that abolishes phosphorylation, thereby preventing intramolecular interaction between the C-terminus and the SH2 domain of c-Src (Upstate Biotechnology, Lake Placid, NY, USA).



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