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DuPont de Nemours α 32 p atp nen dupont
α 32 P Atp Nen Dupont, supplied by DuPont de Nemours, used in various techniques. Bioz Stars score: 81/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/α 32 p atp nen dupont/product/DuPont de Nemours
Average 81 stars, based on 1 article reviews
Price from $9.99 to $1999.99
α 32 p atp nen dupont - by Bioz Stars, 2020-04
81/100 stars

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nucleotide phosphohydrolase assay

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Electrophoresis:

Article Title: A protein tyrosine phosphatase-like protein from baculovirus has RNA 5?-triphosphatase and diphosphatase activities
Article Snippet: To separate monophosphate-terminated oligoribonucleotide ( p ApCpC) from released phosphate ( Pi ), the reaction products were resolved by electrophoresis on a 25% polyacrylamide—3 M urea gel. .. For the nucleotide phosphohydrolase assay, 5 μM [α-32 P] ATP (NEN/DuPont) was used as substrate.

Incubation:

Article Title: A protein tyrosine phosphatase-like protein from baculovirus has RNA 5?-triphosphatase and diphosphatase activities
Article Snippet: Incubation was for 5–30 min at 30°C, and the reaction was terminated by the addition of 1 M formic acid. .. For the nucleotide phosphohydrolase assay, 5 μM [α-32 P] ATP (NEN/DuPont) was used as substrate.

Autoradiography:

Article Title: A protein tyrosine phosphatase-like protein from baculovirus has RNA 5?-triphosphatase and diphosphatase activities
Article Snippet: Radioactivity was detected by using a Fuji BasX phosphorimager and/or autoradiography. .. For the nucleotide phosphohydrolase assay, 5 μM [α-32 P] ATP (NEN/DuPont) was used as substrate.

Radioactivity:

Article Title: A protein tyrosine phosphatase-like protein from baculovirus has RNA 5?-triphosphatase and diphosphatase activities
Article Snippet: Radioactivity was detected by using a Fuji BasX phosphorimager and/or autoradiography. .. For the nucleotide phosphohydrolase assay, 5 μM [α-32 P] ATP (NEN/DuPont) was used as substrate.

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  • 93
    DuPont de Nemours α 32 p atp
    BVP leaves a 5′-monophosphate end. The RNA triphosphatase assay was performed with [α- 32 <t>P]ATP-terminated</t> trinucleotide RNA (label is indicated by an asterisk). After incubation for 10 min at 30°C, the reaction mixture was analyzed by ( A ) PEI–cellulose TLC or ( B ) 25% polyacrylamide gel electrophoresis. The positions of ADP- and AMP-terminated RNA trinucleotides were determined by using ADP- and AMP-terminated trimers as standards (not shown). In A , RNA substrate was incubated with the following: buffer (lane 1), the indicated amount of BVP (BVP, lanes 2–4), an active site mutant of BVP [BVP(C119S), lanes 5–7], 1 unit of CIP (lane 8), the C. elegans capping enzyme triphosphatase (Cel-1[1–236], lanes 9–11), or the corresponding active site mutant [Cel-1[1–236](C124S), lanes 12–14]. Reactions in lanes 1–5 of B were identical to those in lanes 1–4 and 8 of A .
    α 32 P Atp, supplied by DuPont de Nemours, 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/result/α 32 p atp/product/DuPont de Nemours
    Average 93 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    α 32 p atp - by Bioz Stars, 2020-04
    93/100 stars
      Buy from Supplier

    85
    DuPont de Nemours α 32 p ddatp
    BVP leaves a 5′-monophosphate end. The RNA triphosphatase assay was performed with [α- 32 <t>P]ATP-terminated</t> trinucleotide RNA (label is indicated by an asterisk). After incubation for 10 min at 30°C, the reaction mixture was analyzed by ( A ) PEI–cellulose TLC or ( B ) 25% polyacrylamide gel electrophoresis. The positions of ADP- and AMP-terminated RNA trinucleotides were determined by using ADP- and AMP-terminated trimers as standards (not shown). In A , RNA substrate was incubated with the following: buffer (lane 1), the indicated amount of BVP (BVP, lanes 2–4), an active site mutant of BVP [BVP(C119S), lanes 5–7], 1 unit of CIP (lane 8), the C. elegans capping enzyme triphosphatase (Cel-1[1–236], lanes 9–11), or the corresponding active site mutant [Cel-1[1–236](C124S), lanes 12–14]. Reactions in lanes 1–5 of B were identical to those in lanes 1–4 and 8 of A .
    α 32 P Ddatp, supplied by DuPont de Nemours, 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/α 32 p ddatp/product/DuPont de Nemours
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α 32 p ddatp - by Bioz Stars, 2020-04
    85/100 stars
      Buy from Supplier

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    BVP leaves a 5′-monophosphate end. The RNA triphosphatase assay was performed with [α- 32 P]ATP-terminated trinucleotide RNA (label is indicated by an asterisk). After incubation for 10 min at 30°C, the reaction mixture was analyzed by ( A ) PEI–cellulose TLC or ( B ) 25% polyacrylamide gel electrophoresis. The positions of ADP- and AMP-terminated RNA trinucleotides were determined by using ADP- and AMP-terminated trimers as standards (not shown). In A , RNA substrate was incubated with the following: buffer (lane 1), the indicated amount of BVP (BVP, lanes 2–4), an active site mutant of BVP [BVP(C119S), lanes 5–7], 1 unit of CIP (lane 8), the C. elegans capping enzyme triphosphatase (Cel-1[1–236], lanes 9–11), or the corresponding active site mutant [Cel-1[1–236](C124S), lanes 12–14]. Reactions in lanes 1–5 of B were identical to those in lanes 1–4 and 8 of A .

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

    Article Title: A protein tyrosine phosphatase-like protein from baculovirus has RNA 5?-triphosphatase and diphosphatase activities

    doi:

    Figure Lengend Snippet: BVP leaves a 5′-monophosphate end. The RNA triphosphatase assay was performed with [α- 32 P]ATP-terminated trinucleotide RNA (label is indicated by an asterisk). After incubation for 10 min at 30°C, the reaction mixture was analyzed by ( A ) PEI–cellulose TLC or ( B ) 25% polyacrylamide gel electrophoresis. The positions of ADP- and AMP-terminated RNA trinucleotides were determined by using ADP- and AMP-terminated trimers as standards (not shown). In A , RNA substrate was incubated with the following: buffer (lane 1), the indicated amount of BVP (BVP, lanes 2–4), an active site mutant of BVP [BVP(C119S), lanes 5–7], 1 unit of CIP (lane 8), the C. elegans capping enzyme triphosphatase (Cel-1[1–236], lanes 9–11), or the corresponding active site mutant [Cel-1[1–236](C124S), lanes 12–14]. Reactions in lanes 1–5 of B were identical to those in lanes 1–4 and 8 of A .

    Article Snippet: The standard reaction (100 μl) contained 40 mM Tris⋅HCl (pH 7.5), 10 mM MgCl2 , 10 mM DTT, 50 μg/ml BSA, 50 mM potassium glutamate, 2 mM dTTP, 2 mM CTP, 0.3 mM [γ-32 P]- or [α-32 P]ATP (500–1,000 cpm/pmol) (NEN/DuPont), 1 nM DNA template [5′-CCCCCGGTC(T)25 -3′], and 1 μM (hexamer) T7 primase.

    Techniques: Incubation, Thin Layer Chromatography, Polyacrylamide Gel Electrophoresis, Mutagenesis

    Biochemical analysis of signaling responses to AdV, MyD88, and MyD88/TRIF agonists. (A) Western blot analysis of signal transduction using the indicated antibodies. At each indicated time point, whole-cell lysates from mock-treated macrophages were compared to lysates from macrophages stimulated with either 25,000 AdV particles/cell, 10 ng/ml LPS, or 2 μM CpG DNA. Data are representative of three independent experiments. (B) NF-κB gel shift assay. Nuclear extracts from macrophages stimulated for the indicated times were used in gel shift assay with an [α- 32 P]ATP-labeled probe containing a consensus NF-κB-binding sequence.

    Journal: Journal of Virology

    Article Title: Sensing Infection by Adenovirus: Toll-Like Receptor-Independent Viral DNA Recognition Signals Activation of the Interferon Regulatory Factor 3 Master Regulator ▿

    doi: 10.1128/JVI.02685-06

    Figure Lengend Snippet: Biochemical analysis of signaling responses to AdV, MyD88, and MyD88/TRIF agonists. (A) Western blot analysis of signal transduction using the indicated antibodies. At each indicated time point, whole-cell lysates from mock-treated macrophages were compared to lysates from macrophages stimulated with either 25,000 AdV particles/cell, 10 ng/ml LPS, or 2 μM CpG DNA. Data are representative of three independent experiments. (B) NF-κB gel shift assay. Nuclear extracts from macrophages stimulated for the indicated times were used in gel shift assay with an [α- 32 P]ATP-labeled probe containing a consensus NF-κB-binding sequence.

    Article Snippet: Probe labeling was carried out according to the manufacturer's instructions, using [α-32 P]ATP (3,000 Ci/mmol, 10 mCi/ml; DuPont NEN Research Products).

    Techniques: Western Blot, Transduction, Electrophoretic Mobility Shift Assay, Labeling, Binding Assay, Sequencing