proteinase k Roche Search Results


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  • 99
    Thermo Fisher proteinase k
    Proteinase K, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 16083 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Roche proteinase k phosphostop
    Proteinase K Phosphostop, supplied by Roche, used in various techniques. Bioz Stars score: 88/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche protease k
    Protease K, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 226 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Roche proteinase k kit
    Proteinase K Kit, supplied by Roche, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche recombinant proteinase k
    Recombinant Proteinase K, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 97 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Roche protease k pk
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Protease K Pk, supplied by Roche, used in various techniques. Bioz Stars score: 82/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Roche pcr grade proteinase k
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Pcr Grade Proteinase K, supplied by Roche, used in various techniques. Bioz Stars score: 95/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Roche dna free proteinase k
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Dna Free Proteinase K, supplied by Roche, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Roche rnase free proteinase k
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Rnase Free Proteinase K, supplied by Roche, used in various techniques. Bioz Stars score: 78/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Roche proteinase k buffer
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Proteinase K Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 94/100, based on 180 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Roche protease k solution
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Protease K Solution, supplied by Roche, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Roche proteinase k inhibitor
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Proteinase K Inhibitor, supplied by Roche, used in various techniques. Bioz Stars score: 78/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Roche proteinase k dna
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Proteinase K Dna, supplied by Roche, used in various techniques. Bioz Stars score: 97/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    76
    Roche proteinase k sodium dodecyl sulfate
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Proteinase K Sodium Dodecyl Sulfate, supplied by Roche, used in various techniques. Bioz Stars score: 76/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Roche recombinant proteinase k pcr grade
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Recombinant Proteinase K Pcr Grade, supplied by Roche, used in various techniques. Bioz Stars score: 84/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Roche pcr grade recombinant proteinase k solution
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Pcr Grade Recombinant Proteinase K Solution, supplied by Roche, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Roche proteinase k roche dnase free rnase roche aliquot stocks
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Proteinase K Roche Dnase Free Rnase Roche Aliquot Stocks, supplied by Roche, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Roche methanol pbt
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Methanol Pbt, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Roche dna lysis buffer
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Dna Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Roche dna extraction buffer
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Dna Extraction Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 84/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Roche ras extraction kit
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Ras Extraction Kit, supplied by Roche, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Roche digestion buffer
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Digestion Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 97/100, based on 1156 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Roche stop buffer
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Stop Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 94/100, based on 167 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Roche lysis solution
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Lysis Solution, supplied by Roche, used in various techniques. Bioz Stars score: 96/100, based on 530 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Roche antigen retrieval
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Antigen Retrieval, supplied by Roche, used in various techniques. Bioz Stars score: 96/100, based on 715 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Roche chip elution buffer
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Chip Elution Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 87/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche extraction buffer
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Extraction Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 6450 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche lysis buffer
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 103639 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
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    Roche high pure ffpe rna micro kit
    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of <t>protease</t> K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.
    High Pure Ffpe Rna Micro Kit, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 393 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of protease K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.

    Journal: Journal of Virology

    Article Title: In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding

    doi: 10.1128/JVI.01543-17

    Figure Lengend Snippet: Biochemical characterization of mutated rabbit rec-PrP-containing substrates showed similar amounts of rec-PrP present. The Western blot shows similar amounts of the different recPMCA substrates based on wild-type rabbit rec-PrPs (wt rPrP) with specific mouse substitutions. Note the presence of a single band of approximately 20 kDa in the absence of protease K (PK) treatment. Wild-type rabbit and mouse rec-PrP-containing substrates are also included. The lower signal for the wild-type mouse rec-PrP (mouse rPrP) can be explained by a lower affinity of the monoclonal antibody SAF84 (1:400) which was used to develop the membranes. Rabbit PrP C (rabbit normal brain homogenate) was run in a separate gel, and the image is shown divided from the other gel by a vertical gray line.

    Article Snippet: recPMCA-treated samples were incubated with 25 μg/ml of protease K (PK) (Roche) for 1 h at 42°C and with constant agitation at 450 rpm (Thermomixer Comfort; Eppendorf) as described previously ( ).

    Techniques: Western Blot

    Three of 11 recombinant rabbit PrPs with mouse PrP single-residue substitutions were misfolded by recRML and brainRML murine prions  in vitro . (A) Graphical representation of the emergence and relative amount of protein misfolding (PrP res ) for each round of recPMCA (denoted R01 to R20) as evaluated by Western blotting and SDS-PAGE. The percentages of tubes showing PK-resistant misfolded rec-PrP are indicated in grayscale according to the legend. Different mutated rabbit recombinant proteins were subjected to serial rounds of recPMCA after seeding with recRML (misfolded recombinant mouse PrP [recRML-High]). Note the spontaneous emergence of misfolding for the unseeded S107N variant. WT, wild-type rabbit rec-PrPs. (B) Selected mutated rabbit recombinant proteins were subjected to serial rounds of recPMCA after seeding with brainRML (brain-derived RML). Every experiment contained 4 tubes (intraexperimental replicates). The percentage of positive tubes (tubes showing a protease K-resistant signal after digestion with 80 μg/ml of PK) after each round of recPMCA is noted in grayscale as shown in the legend. (C) Western blot representing the recRML (recombinant origin)- or brainRML (brain origin)-seeded and misfolded mutated rabbit rec-PrPs after PK digestion. Samples were digested with 85 μg/ml of PK. Similar bands of approximately 17 kDa, corresponding to the PK-resistant 90-230 fragment of the prion protein, are shown. Membranes were developed with monoclonal antibody SAF84 (1:400). Rabbit rPrP, undigested recombinant rabbit rec-PrP.

    Journal: Journal of Virology

    Article Title: In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding

    doi: 10.1128/JVI.01543-17

    Figure Lengend Snippet: Three of 11 recombinant rabbit PrPs with mouse PrP single-residue substitutions were misfolded by recRML and brainRML murine prions in vitro . (A) Graphical representation of the emergence and relative amount of protein misfolding (PrP res ) for each round of recPMCA (denoted R01 to R20) as evaluated by Western blotting and SDS-PAGE. The percentages of tubes showing PK-resistant misfolded rec-PrP are indicated in grayscale according to the legend. Different mutated rabbit recombinant proteins were subjected to serial rounds of recPMCA after seeding with recRML (misfolded recombinant mouse PrP [recRML-High]). Note the spontaneous emergence of misfolding for the unseeded S107N variant. WT, wild-type rabbit rec-PrPs. (B) Selected mutated rabbit recombinant proteins were subjected to serial rounds of recPMCA after seeding with brainRML (brain-derived RML). Every experiment contained 4 tubes (intraexperimental replicates). The percentage of positive tubes (tubes showing a protease K-resistant signal after digestion with 80 μg/ml of PK) after each round of recPMCA is noted in grayscale as shown in the legend. (C) Western blot representing the recRML (recombinant origin)- or brainRML (brain origin)-seeded and misfolded mutated rabbit rec-PrPs after PK digestion. Samples were digested with 85 μg/ml of PK. Similar bands of approximately 17 kDa, corresponding to the PK-resistant 90-230 fragment of the prion protein, are shown. Membranes were developed with monoclonal antibody SAF84 (1:400). Rabbit rPrP, undigested recombinant rabbit rec-PrP.

    Article Snippet: recPMCA-treated samples were incubated with 25 μg/ml of protease K (PK) (Roche) for 1 h at 42°C and with constant agitation at 450 rpm (Thermomixer Comfort; Eppendorf) as described previously ( ).

    Techniques: Recombinant, In Vitro, Western Blot, SDS Page, Variant Assay, Derivative Assay

    Mutated rabbit rec-PrPs that are more susceptible to misfolding by RML are also susceptible to prions from other species. The diagram shows rec-PrP res generation over the course of serial in vitro propagation of ME7, scrapie (SSBP/1), sheep BSE (ShBSE), and classical BSE inocula on substrates containing mutated rabbit rec-PrPs (S107N, M108L, and I202V) selected because of their higher propensity to be misfolded by mouse RML. Generation of rec-PrP res was evaluated by protease K (PK) digestion and Western blotting (with monoclonal antibody SAF84) for each recPMCA round (rounds 1 to 20). Wild-type rabbit (RaWt) and wild-type mouse (MoWt) rec-PrP-containing substrates were included as negative and positive controls, respectively. Note that wild-type mouse recombinant PrP was the most susceptible to misfolding by all the seeds used, as expected, while recombinant rabbit PrP was again unable to be misfolded. Regarding the mutated rabbit rec-PrPs, despite all being misfolded by all of the seeds used, the I202V mutant showed, in most cases, the greatest percentage of misfolded tubes and earlier affected rounds, suggesting that it is the most susceptible to misfolding by all of the seeds used. The percentages of tubes showing PK-resistant misfolded rec-PrP are indicated in greyscale according to the legend.

    Journal: Journal of Virology

    Article Title: In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding

    doi: 10.1128/JVI.01543-17

    Figure Lengend Snippet: Mutated rabbit rec-PrPs that are more susceptible to misfolding by RML are also susceptible to prions from other species. The diagram shows rec-PrP res generation over the course of serial in vitro propagation of ME7, scrapie (SSBP/1), sheep BSE (ShBSE), and classical BSE inocula on substrates containing mutated rabbit rec-PrPs (S107N, M108L, and I202V) selected because of their higher propensity to be misfolded by mouse RML. Generation of rec-PrP res was evaluated by protease K (PK) digestion and Western blotting (with monoclonal antibody SAF84) for each recPMCA round (rounds 1 to 20). Wild-type rabbit (RaWt) and wild-type mouse (MoWt) rec-PrP-containing substrates were included as negative and positive controls, respectively. Note that wild-type mouse recombinant PrP was the most susceptible to misfolding by all the seeds used, as expected, while recombinant rabbit PrP was again unable to be misfolded. Regarding the mutated rabbit rec-PrPs, despite all being misfolded by all of the seeds used, the I202V mutant showed, in most cases, the greatest percentage of misfolded tubes and earlier affected rounds, suggesting that it is the most susceptible to misfolding by all of the seeds used. The percentages of tubes showing PK-resistant misfolded rec-PrP are indicated in greyscale according to the legend.

    Article Snippet: recPMCA-treated samples were incubated with 25 μg/ml of protease K (PK) (Roche) for 1 h at 42°C and with constant agitation at 450 rpm (Thermomixer Comfort; Eppendorf) as described previously ( ).

    Techniques: In Vitro, Western Blot, Recombinant, Mutagenesis