Structured Review

ICN Pharmaceuticals α 32 p atp
α 32 P Atp, supplied by ICN Pharmaceuticals, 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 atp/product/ICN Pharmaceuticals
Average 85 stars, based on 1 article reviews
Price from $9.99 to $1999.99
α 32 p atp - by Bioz Stars, 2020-04
85/100 stars

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Mutagenesis:

Article Title: Characterization of Pneumocystis carinii PHR1, a pH-Regulated Gene Important for Cell Wall Integrity
Article Snippet: [α-32 P]ATP was obtained from ICN Pharmaceuticals (Costa Mesa, Calif.). .. The WB2d Saccharomyces cerevisiae strain expressing a mutated and ineffective Gas1p (YEp- gas1 mutant) was the generous gift of Marina Vai, Università degli Studi di Milano, Milan, Italy ( ).

Construct:

Article Title: Characterization of Pneumocystis carinii PHR1, a pH-Regulated Gene Important for Cell Wall Integrity
Article Snippet: [α-32 P]ATP was obtained from ICN Pharmaceuticals (Costa Mesa, Calif.). .. The yeast expression plasmid p425GAL used in the generation of the p425GAL -PHR1 construct was obtained from the American Type Culture Collection (Rockville, Md.).

Purification:

Article Title: Mitochondrial Localization of the Mevalonate Pathway Enzyme 3-Hydroxy-3-methyl-glutaryl-CoA Reductase in the Trypanosomatidae
Article Snippet: [α-32 P]ATP was from ICN Pharmaceuticals (Irvine, CA). d , l -[3-14 C]3-hydroxy-3-methylglutaryl-CoA was from Amersham Biosciences (Piscataway, NJ), and R,S -[5-3 H(N)]mevalonolactone was from DuPont (Wilmington, DE). .. The mRNA purification kit was from Pharmacia (Peapack, NJ).

Expressing:

Article Title: Characterization of Pneumocystis carinii PHR1, a pH-Regulated Gene Important for Cell Wall Integrity
Article Snippet: [α-32 P]ATP was obtained from ICN Pharmaceuticals (Costa Mesa, Calif.). .. The WB2d Saccharomyces cerevisiae strain expressing a mutated and ineffective Gas1p (YEp- gas1 mutant) was the generous gift of Marina Vai, Università degli Studi di Milano, Milan, Italy ( ).

Plasmid Preparation:

Article Title: Characterization of Pneumocystis carinii PHR1, a pH-Regulated Gene Important for Cell Wall Integrity
Article Snippet: [α-32 P]ATP was obtained from ICN Pharmaceuticals (Costa Mesa, Calif.). .. The plasmid YEp- GAS1, containing the wild-type GAS1 gene used as a complementation control, was also obtained from M. Vai.

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  • 81
    ICN Pharmaceuticals 8 azido
    Arp2p and Arp3p are ATP-binding proteins. (A) Arp2p and Arp3p were labeled by <t>8-azido-[α-</t> 32 P]ATP. Wild-type cells carrying pRMH42 arp2 + (KGY2224), pRMH42 arp2 -E316K (KGY2225), or pRMH42 arp2 -T12A (KGY2226) were grown to midlog phase in minimal medium containing thiamine at 25°C, washed to remove the thiamine, and then incubated for 22 h at 25°C to induce expression of the myc-tagged Arp2 proteins. After cell lysis under native conditions, the myc-tagged Arp2 proteins were immunoprecipitated and then mixed with 2 μM 8-azido-[α- 32 P]ATP. Samples were subjected to UV irradiation to promote cross-linking between Arp2p and 8-azido-[α- 32 P]ATP. After irradiation, a fraction of each sample was denatured by boiling, and a second immunoprecipitation was performed with the use of either anti-Arp2 or anti-Arp3 antibodies to distinguish between myc-Arp2p and Arp3p. Cold ATP was added to a final concentration of 500 μM in competition experiments. Labeled proteins were resolved by SDS-PAGE and autoradiography. (B) Immunoprecipitation of myc-tagged Arp2 proteins from lysates used in ATP-binding assays with the 9E10 anti-myc mAb. (Lane 1) Wild type (KGY28); (lane 2) pRMH42 arp2 + (KGY2224); (lane 3) pRMH42 arp2 -E316K (KGY2225); (lane 4) pRMH42 arp2 -T12A (KGY2226). Immunoblots were probed with 9E10 anti-myc antibody to detect tagged Arp2. (C) After induction of myc-tagged wild-type Arp2 (KGY2224) and Arp2-E316K (KGY2225) in wild-type cells for 20 h at 32°C, thiamine was added back to the culture medium to repress expression of the tagged Arp2 proteins from the nmt1 promoter. Lysates were prepared from cells collected hourly after transcriptional repression, and the myc-tagged Arp2 proteins, along with endogenous Arp2p (loading control), were detected by immunoblotting with the use of anti-Arp2 antibodies. (D) myc-tagged Arp2 proteins were immunoprecipitated from native lysates and resolved by SDS-PAGE. (Lane 1) Wild-type (KGY28); (lane 2) pRMH42 arp2 + (KGY2224); (lane 3) pRMH42 arp2 -E316K (KGY2225); (lane 4) pRMH42 arp2 -T12A (KGY2226). The presence of coimmunoprecipitated Arp3p was detected by immunoblotting with the use of anti-Arp3p antibodies.
    8 Azido, supplied by ICN Pharmaceuticals, 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/8 azido/product/ICN Pharmaceuticals
    Average 81 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    8 azido - by Bioz Stars, 2020-04
    81/100 stars
      Buy from Supplier

    85
    ICN Pharmaceuticals α 32 p atp
    Arp2p and Arp3p are ATP-binding proteins. (A) Arp2p and Arp3p were labeled by <t>8-azido-[α-</t> 32 P]ATP. Wild-type cells carrying pRMH42 arp2 + (KGY2224), pRMH42 arp2 -E316K (KGY2225), or pRMH42 arp2 -T12A (KGY2226) were grown to midlog phase in minimal medium containing thiamine at 25°C, washed to remove the thiamine, and then incubated for 22 h at 25°C to induce expression of the myc-tagged Arp2 proteins. After cell lysis under native conditions, the myc-tagged Arp2 proteins were immunoprecipitated and then mixed with 2 μM 8-azido-[α- 32 P]ATP. Samples were subjected to UV irradiation to promote cross-linking between Arp2p and 8-azido-[α- 32 P]ATP. After irradiation, a fraction of each sample was denatured by boiling, and a second immunoprecipitation was performed with the use of either anti-Arp2 or anti-Arp3 antibodies to distinguish between myc-Arp2p and Arp3p. Cold ATP was added to a final concentration of 500 μM in competition experiments. Labeled proteins were resolved by SDS-PAGE and autoradiography. (B) Immunoprecipitation of myc-tagged Arp2 proteins from lysates used in ATP-binding assays with the 9E10 anti-myc mAb. (Lane 1) Wild type (KGY28); (lane 2) pRMH42 arp2 + (KGY2224); (lane 3) pRMH42 arp2 -E316K (KGY2225); (lane 4) pRMH42 arp2 -T12A (KGY2226). Immunoblots were probed with 9E10 anti-myc antibody to detect tagged Arp2. (C) After induction of myc-tagged wild-type Arp2 (KGY2224) and Arp2-E316K (KGY2225) in wild-type cells for 20 h at 32°C, thiamine was added back to the culture medium to repress expression of the tagged Arp2 proteins from the nmt1 promoter. Lysates were prepared from cells collected hourly after transcriptional repression, and the myc-tagged Arp2 proteins, along with endogenous Arp2p (loading control), were detected by immunoblotting with the use of anti-Arp2 antibodies. (D) myc-tagged Arp2 proteins were immunoprecipitated from native lysates and resolved by SDS-PAGE. (Lane 1) Wild-type (KGY28); (lane 2) pRMH42 arp2 + (KGY2224); (lane 3) pRMH42 arp2 -E316K (KGY2225); (lane 4) pRMH42 arp2 -T12A (KGY2226). The presence of coimmunoprecipitated Arp3p was detected by immunoblotting with the use of anti-Arp3p antibodies.
    α 32 P Atp, supplied by ICN Pharmaceuticals, 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 atp/product/ICN Pharmaceuticals
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α 32 p atp - by Bioz Stars, 2020-04
    85/100 stars
      Buy from Supplier

    Image Search Results


    Arp2p and Arp3p are ATP-binding proteins. (A) Arp2p and Arp3p were labeled by 8-azido-[α- 32 P]ATP. Wild-type cells carrying pRMH42 arp2 + (KGY2224), pRMH42 arp2 -E316K (KGY2225), or pRMH42 arp2 -T12A (KGY2226) were grown to midlog phase in minimal medium containing thiamine at 25°C, washed to remove the thiamine, and then incubated for 22 h at 25°C to induce expression of the myc-tagged Arp2 proteins. After cell lysis under native conditions, the myc-tagged Arp2 proteins were immunoprecipitated and then mixed with 2 μM 8-azido-[α- 32 P]ATP. Samples were subjected to UV irradiation to promote cross-linking between Arp2p and 8-azido-[α- 32 P]ATP. After irradiation, a fraction of each sample was denatured by boiling, and a second immunoprecipitation was performed with the use of either anti-Arp2 or anti-Arp3 antibodies to distinguish between myc-Arp2p and Arp3p. Cold ATP was added to a final concentration of 500 μM in competition experiments. Labeled proteins were resolved by SDS-PAGE and autoradiography. (B) Immunoprecipitation of myc-tagged Arp2 proteins from lysates used in ATP-binding assays with the 9E10 anti-myc mAb. (Lane 1) Wild type (KGY28); (lane 2) pRMH42 arp2 + (KGY2224); (lane 3) pRMH42 arp2 -E316K (KGY2225); (lane 4) pRMH42 arp2 -T12A (KGY2226). Immunoblots were probed with 9E10 anti-myc antibody to detect tagged Arp2. (C) After induction of myc-tagged wild-type Arp2 (KGY2224) and Arp2-E316K (KGY2225) in wild-type cells for 20 h at 32°C, thiamine was added back to the culture medium to repress expression of the tagged Arp2 proteins from the nmt1 promoter. Lysates were prepared from cells collected hourly after transcriptional repression, and the myc-tagged Arp2 proteins, along with endogenous Arp2p (loading control), were detected by immunoblotting with the use of anti-Arp2 antibodies. (D) myc-tagged Arp2 proteins were immunoprecipitated from native lysates and resolved by SDS-PAGE. (Lane 1) Wild-type (KGY28); (lane 2) pRMH42 arp2 + (KGY2224); (lane 3) pRMH42 arp2 -E316K (KGY2225); (lane 4) pRMH42 arp2 -T12A (KGY2226). The presence of coimmunoprecipitated Arp3p was detected by immunoblotting with the use of anti-Arp3p antibodies.

    Journal: Molecular Biology of the Cell

    Article Title: A Mutant of Arp2p Causes Partial Disassembly of the Arp2/3 Complex and Loss of Cortical Actin Function in Fission Yeast

    doi:

    Figure Lengend Snippet: Arp2p and Arp3p are ATP-binding proteins. (A) Arp2p and Arp3p were labeled by 8-azido-[α- 32 P]ATP. Wild-type cells carrying pRMH42 arp2 + (KGY2224), pRMH42 arp2 -E316K (KGY2225), or pRMH42 arp2 -T12A (KGY2226) were grown to midlog phase in minimal medium containing thiamine at 25°C, washed to remove the thiamine, and then incubated for 22 h at 25°C to induce expression of the myc-tagged Arp2 proteins. After cell lysis under native conditions, the myc-tagged Arp2 proteins were immunoprecipitated and then mixed with 2 μM 8-azido-[α- 32 P]ATP. Samples were subjected to UV irradiation to promote cross-linking between Arp2p and 8-azido-[α- 32 P]ATP. After irradiation, a fraction of each sample was denatured by boiling, and a second immunoprecipitation was performed with the use of either anti-Arp2 or anti-Arp3 antibodies to distinguish between myc-Arp2p and Arp3p. Cold ATP was added to a final concentration of 500 μM in competition experiments. Labeled proteins were resolved by SDS-PAGE and autoradiography. (B) Immunoprecipitation of myc-tagged Arp2 proteins from lysates used in ATP-binding assays with the 9E10 anti-myc mAb. (Lane 1) Wild type (KGY28); (lane 2) pRMH42 arp2 + (KGY2224); (lane 3) pRMH42 arp2 -E316K (KGY2225); (lane 4) pRMH42 arp2 -T12A (KGY2226). Immunoblots were probed with 9E10 anti-myc antibody to detect tagged Arp2. (C) After induction of myc-tagged wild-type Arp2 (KGY2224) and Arp2-E316K (KGY2225) in wild-type cells for 20 h at 32°C, thiamine was added back to the culture medium to repress expression of the tagged Arp2 proteins from the nmt1 promoter. Lysates were prepared from cells collected hourly after transcriptional repression, and the myc-tagged Arp2 proteins, along with endogenous Arp2p (loading control), were detected by immunoblotting with the use of anti-Arp2 antibodies. (D) myc-tagged Arp2 proteins were immunoprecipitated from native lysates and resolved by SDS-PAGE. (Lane 1) Wild-type (KGY28); (lane 2) pRMH42 arp2 + (KGY2224); (lane 3) pRMH42 arp2 -E316K (KGY2225); (lane 4) pRMH42 arp2 -T12A (KGY2226). The presence of coimmunoprecipitated Arp3p was detected by immunoblotting with the use of anti-Arp3p antibodies.

    Article Snippet: Photoaffinity labeling was carried out by mixing immunoprecipitated protein and 2 μM 8-azido-[α-32 P]ATP (20 Ci/mmol; ICN Pharmaceuticals) in a total volume of 100 μl.

    Techniques: Binding Assay, Labeling, Incubation, Expressing, Lysis, Immunoprecipitation, Irradiation, Concentration Assay, SDS Page, Autoradiography, Western Blot