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    Roche immunoprecipitation buffer
    <t>Immunoprecipitation</t> of mutant PfSec22 and PfARO proteins using antibodies against the c‐Myc tag. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of mutant c‐Myc‐tagged PfSec22 or PfARO (which had the predicted palmitoylated cysteine residues mutated to alanine residues), along with FLAG‐tagged PfDHHC5 or the control vector (CD4). The mutant PfSec22 and PfARO proteins were immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. A. Immunoprecipitation of PfSec22 point mutants (PfSec22‐C2dA, PfSec22‐C8dA and PfSec22‐C2C8dA) along with wild‐type PfSec22. The amino acid sequence of the N‐terminal region of PfSec22 is also shown with the cysteine residues of interest highlighted in red. B. Immunoprecipitation of PfARO point mutants (PfARO‐C5dA, PfARO‐C6dA and PfARO‐C5C6dA) along with wild‐type PfARO. The amino acid sequence of the N‐terminal region of PfARO is also shown with the cysteine residues of interest highlighted in red.
    Immunoprecipitation Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/immunoprecipitation buffer/product/Roche
    Average 86 stars, based on 1 article reviews
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    immunoprecipitation buffer - by Bioz Stars, 2021-06
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    99
    Millipore radioimmunoprecipitation assay buffer
    <t>Immunoprecipitation</t> of mutant PfSec22 and PfARO proteins using antibodies against the c‐Myc tag. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of mutant c‐Myc‐tagged PfSec22 or PfARO (which had the predicted palmitoylated cysteine residues mutated to alanine residues), along with FLAG‐tagged PfDHHC5 or the control vector (CD4). The mutant PfSec22 and PfARO proteins were immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. A. Immunoprecipitation of PfSec22 point mutants (PfSec22‐C2dA, PfSec22‐C8dA and PfSec22‐C2C8dA) along with wild‐type PfSec22. The amino acid sequence of the N‐terminal region of PfSec22 is also shown with the cysteine residues of interest highlighted in red. B. Immunoprecipitation of PfARO point mutants (PfARO‐C5dA, PfARO‐C6dA and PfARO‐C5C6dA) along with wild‐type PfARO. The amino acid sequence of the N‐terminal region of PfARO is also shown with the cysteine residues of interest highlighted in red.
    Radioimmunoprecipitation Assay Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/radioimmunoprecipitation assay buffer/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    radioimmunoprecipitation assay buffer - by Bioz Stars, 2021-06
    99/100 stars
      Buy from Supplier

    86
    Beyotime radioimmunoprecipitation assay lysis buffer
    <t>Immunoprecipitation</t> of mutant PfSec22 and PfARO proteins using antibodies against the c‐Myc tag. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of mutant c‐Myc‐tagged PfSec22 or PfARO (which had the predicted palmitoylated cysteine residues mutated to alanine residues), along with FLAG‐tagged PfDHHC5 or the control vector (CD4). The mutant PfSec22 and PfARO proteins were immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. A. Immunoprecipitation of PfSec22 point mutants (PfSec22‐C2dA, PfSec22‐C8dA and PfSec22‐C2C8dA) along with wild‐type PfSec22. The amino acid sequence of the N‐terminal region of PfSec22 is also shown with the cysteine residues of interest highlighted in red. B. Immunoprecipitation of PfARO point mutants (PfARO‐C5dA, PfARO‐C6dA and PfARO‐C5C6dA) along with wild‐type PfARO. The amino acid sequence of the N‐terminal region of PfARO is also shown with the cysteine residues of interest highlighted in red.
    Radioimmunoprecipitation Assay Lysis Buffer, supplied by Beyotime, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/radioimmunoprecipitation assay lysis buffer/product/Beyotime
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    radioimmunoprecipitation assay lysis buffer - by Bioz Stars, 2021-06
    86/100 stars
      Buy from Supplier

    99
    Millipore immunoprecipitation buffer
    <t>Immunoprecipitation</t> of mutant PfSec22 and PfARO proteins using antibodies against the c‐Myc tag. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of mutant c‐Myc‐tagged PfSec22 or PfARO (which had the predicted palmitoylated cysteine residues mutated to alanine residues), along with FLAG‐tagged PfDHHC5 or the control vector (CD4). The mutant PfSec22 and PfARO proteins were immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. A. Immunoprecipitation of PfSec22 point mutants (PfSec22‐C2dA, PfSec22‐C8dA and PfSec22‐C2C8dA) along with wild‐type PfSec22. The amino acid sequence of the N‐terminal region of PfSec22 is also shown with the cysteine residues of interest highlighted in red. B. Immunoprecipitation of PfARO point mutants (PfARO‐C5dA, PfARO‐C6dA and PfARO‐C5C6dA) along with wild‐type PfARO. The amino acid sequence of the N‐terminal region of PfARO is also shown with the cysteine residues of interest highlighted in red.
    Immunoprecipitation Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/immunoprecipitation buffer/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    immunoprecipitation buffer - by Bioz Stars, 2021-06
    99/100 stars
      Buy from Supplier


    Image Search Results


    Immunoprecipitation of mutant PfSec22 and PfARO proteins using antibodies against the c‐Myc tag. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of mutant c‐Myc‐tagged PfSec22 or PfARO (which had the predicted palmitoylated cysteine residues mutated to alanine residues), along with FLAG‐tagged PfDHHC5 or the control vector (CD4). The mutant PfSec22 and PfARO proteins were immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. A. Immunoprecipitation of PfSec22 point mutants (PfSec22‐C2dA, PfSec22‐C8dA and PfSec22‐C2C8dA) along with wild‐type PfSec22. The amino acid sequence of the N‐terminal region of PfSec22 is also shown with the cysteine residues of interest highlighted in red. B. Immunoprecipitation of PfARO point mutants (PfARO‐C5dA, PfARO‐C6dA and PfARO‐C5C6dA) along with wild‐type PfARO. The amino acid sequence of the N‐terminal region of PfARO is also shown with the cysteine residues of interest highlighted in red.

    Journal: Cellular Microbiology

    Article Title: Study of Plasmodium falciparum DHHC palmitoyl transferases identifies a role for PfDHHC9 in gametocytogenesis) Study of Plasmodium falciparum DHHC palmitoyl transferases identifies a role for PfDHHC9 in gametocytogenesis

    doi: 10.1111/cmi.12599

    Figure Lengend Snippet: Immunoprecipitation of mutant PfSec22 and PfARO proteins using antibodies against the c‐Myc tag. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of mutant c‐Myc‐tagged PfSec22 or PfARO (which had the predicted palmitoylated cysteine residues mutated to alanine residues), along with FLAG‐tagged PfDHHC5 or the control vector (CD4). The mutant PfSec22 and PfARO proteins were immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. A. Immunoprecipitation of PfSec22 point mutants (PfSec22‐C2dA, PfSec22‐C8dA and PfSec22‐C2C8dA) along with wild‐type PfSec22. The amino acid sequence of the N‐terminal region of PfSec22 is also shown with the cysteine residues of interest highlighted in red. B. Immunoprecipitation of PfARO point mutants (PfARO‐C5dA, PfARO‐C6dA and PfARO‐C5C6dA) along with wild‐type PfARO. The amino acid sequence of the N‐terminal region of PfARO is also shown with the cysteine residues of interest highlighted in red.

    Article Snippet: For the immunoprecipitation of tagged proteins, cell pellets were lysed in immunoprecipitation buffer [1% Triton X‐100/50 mm Tris‐Cl pH 7.4/150 mm NaCl/5 mm EDTA/protease inhibitor cocktail (Roche)] for 30 min at 37°C with shaking.

    Techniques: Immunoprecipitation, Mutagenesis, Transfection, Expressing, Plasmid Preparation, SDS Page, Sequencing

    Palmitoyl‐transferase activity assay demonstrating the palmitoyl‐transferase activity of the PfDHHC proteins on PfSec22. A. Immunoprecipitation of PfSec22 co‐expressed with each PfDHHC protein. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of c‐Myc‐tagged PfSec22, along with the indicated FLAG‐tagged PfDHHC proteins (PfDHHC3, 5, 7 and 9) or the control vector (CD4). Pfsec22 was immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. B. PAT activity assay. Human embryonic kidney 293E cells were co‐transfected with plasmids expressing c‐Myc‐tagged PfSec22, along with the indicated FLAG‐tagged PfDHHC protein or the control vector (CD4). Cells were either treated with the metabolic label, 17‐octadecynoic acid (17‐ODYA) or mock‐treated with DMSO. Proteins were extracted and an aliquot of each lysate kept aside to confirm protein expression. The remaining lysates were put through click chemistry reactions to biotin‐azide, and 17‐ODYA‐labelled proteins were streptavidin affinity purified and eluted by boiling in SDS. Samples from the initial lysates and the click chemistry elutions were separated by SDS‐PAGE, and the presence of c‐Myc‐tagged PfSec22 in each of the samples was observed by immunoblot using antibodies against the c‐Myc tag.

    Journal: Cellular Microbiology

    Article Title: Study of Plasmodium falciparum DHHC palmitoyl transferases identifies a role for PfDHHC9 in gametocytogenesis) Study of Plasmodium falciparum DHHC palmitoyl transferases identifies a role for PfDHHC9 in gametocytogenesis

    doi: 10.1111/cmi.12599

    Figure Lengend Snippet: Palmitoyl‐transferase activity assay demonstrating the palmitoyl‐transferase activity of the PfDHHC proteins on PfSec22. A. Immunoprecipitation of PfSec22 co‐expressed with each PfDHHC protein. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of c‐Myc‐tagged PfSec22, along with the indicated FLAG‐tagged PfDHHC proteins (PfDHHC3, 5, 7 and 9) or the control vector (CD4). Pfsec22 was immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. B. PAT activity assay. Human embryonic kidney 293E cells were co‐transfected with plasmids expressing c‐Myc‐tagged PfSec22, along with the indicated FLAG‐tagged PfDHHC protein or the control vector (CD4). Cells were either treated with the metabolic label, 17‐octadecynoic acid (17‐ODYA) or mock‐treated with DMSO. Proteins were extracted and an aliquot of each lysate kept aside to confirm protein expression. The remaining lysates were put through click chemistry reactions to biotin‐azide, and 17‐ODYA‐labelled proteins were streptavidin affinity purified and eluted by boiling in SDS. Samples from the initial lysates and the click chemistry elutions were separated by SDS‐PAGE, and the presence of c‐Myc‐tagged PfSec22 in each of the samples was observed by immunoblot using antibodies against the c‐Myc tag.

    Article Snippet: For the immunoprecipitation of tagged proteins, cell pellets were lysed in immunoprecipitation buffer [1% Triton X‐100/50 mm Tris‐Cl pH 7.4/150 mm NaCl/5 mm EDTA/protease inhibitor cocktail (Roche)] for 30 min at 37°C with shaking.

    Techniques: Activity Assay, Immunoprecipitation, Transfection, Expressing, Plasmid Preparation, SDS Page, Affinity Purification

    Palmitoyl‐transferase activity assay demonstrating the palmitoyl‐transferase activity of the PfDHHC proteins on PfARO. A. Immunoprecipitation of PfARO co‐expressed with each PfDHHC protein. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of c‐Myc‐tagged PfARO, along with the indicated FLAG‐tagged PfDHHC proteins (PfDHHC3, 5, 7 and 9) or the control vector (CD4). PfARO was immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. B. PAT activity assay. Human embryonic kidney 293E cells were co‐transfected with plasmids expressing c‐Myc‐tagged PfARO, along with the indicated FLAG‐tagged PfDHHC protein or the control vector, CD4. Cells were either treated with the metabolic label, 17‐octadecynoic acid or mock‐treated with DMSO. Proteins were extracted, and an aliquot of each lysate kept aside to confirm protein expression. The remaining lysates were put through click chemistry reactions to biotin‐azide, and 17‐octadecynoic acid‐labelled proteins were streptavidin affinity purified and eluted by boiling in SDS. Samples from the initial lysates and the click chemistry elutions were separated by SDS‐PAGE, and the presence of c‐Myc‐tagged PfARO in each of the samples was observed by immunoblot using antibodies against the c‐Myc tag.

    Journal: Cellular Microbiology

    Article Title: Study of Plasmodium falciparum DHHC palmitoyl transferases identifies a role for PfDHHC9 in gametocytogenesis) Study of Plasmodium falciparum DHHC palmitoyl transferases identifies a role for PfDHHC9 in gametocytogenesis

    doi: 10.1111/cmi.12599

    Figure Lengend Snippet: Palmitoyl‐transferase activity assay demonstrating the palmitoyl‐transferase activity of the PfDHHC proteins on PfARO. A. Immunoprecipitation of PfARO co‐expressed with each PfDHHC protein. Human embryonic kidney 293E cells were co‐transfected with plasmids coding for the expression of c‐Myc‐tagged PfARO, along with the indicated FLAG‐tagged PfDHHC proteins (PfDHHC3, 5, 7 and 9) or the control vector (CD4). PfARO was immunoprecipitated from cell lysates using α ‐c‐Myc antibody. The proteins were separated by SDS‐PAGE and visualized by immunoblot, using α ‐c‐Myc antibody from a different species. B. PAT activity assay. Human embryonic kidney 293E cells were co‐transfected with plasmids expressing c‐Myc‐tagged PfARO, along with the indicated FLAG‐tagged PfDHHC protein or the control vector, CD4. Cells were either treated with the metabolic label, 17‐octadecynoic acid or mock‐treated with DMSO. Proteins were extracted, and an aliquot of each lysate kept aside to confirm protein expression. The remaining lysates were put through click chemistry reactions to biotin‐azide, and 17‐octadecynoic acid‐labelled proteins were streptavidin affinity purified and eluted by boiling in SDS. Samples from the initial lysates and the click chemistry elutions were separated by SDS‐PAGE, and the presence of c‐Myc‐tagged PfARO in each of the samples was observed by immunoblot using antibodies against the c‐Myc tag.

    Article Snippet: For the immunoprecipitation of tagged proteins, cell pellets were lysed in immunoprecipitation buffer [1% Triton X‐100/50 mm Tris‐Cl pH 7.4/150 mm NaCl/5 mm EDTA/protease inhibitor cocktail (Roche)] for 30 min at 37°C with shaking.

    Techniques: Activity Assay, Immunoprecipitation, Transfection, Expressing, Plasmid Preparation, SDS Page, Affinity Purification