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proteins 695  (Bio-Rad)


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    Structured Review

    Bio-Rad proteins 695
    Proteins 695, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 32538 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/proteins+695/Nitrocellulose+Membrane/pm41309594-313-0-10
    Average 99 stars, based on 32538 article reviews
    proteins 695 - by Bioz Stars, 2026-09
    99/100 stars

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    Related Articles

    Membrane:

    Article Title: An essential adaptor for apicoplast fission and inheritance in malaria parasites.
    Article Snippet: Parasite pellets were resuspended in 692 Laemmli sample buffer + 5% v/v β-mercaptoethanol (Aldrich), heated at 37 °C for 1 hour 693 with vortexing every 30 minutes, and separated by size using BioRad 4-20% Mini-694 PROTEAN TGX stain free gels (BioRad Cat. #4568095) at 200 V for 40 minutes. .. Proteins 695 were transferred to a nitrocellulose membrane using a BioRad Transblot Turbo Transfer 696 System with the MixedMW setting (25 V, 1.3 A, 7 minutes) before blocking using 1:5 697 BioRad EveryBlot Blocking Buffer (BioRad Cat. #12010020): PBS for 30 minutes at room 698 temperature. ..

    Blocking Assay:

    Article Title: An essential adaptor for apicoplast fission and inheritance in malaria parasites.
    Article Snippet: Parasite pellets were resuspended in 692 Laemmli sample buffer + 5% v/v β-mercaptoethanol (Aldrich), heated at 37 °C for 1 hour 693 with vortexing every 30 minutes, and separated by size using BioRad 4-20% Mini-694 PROTEAN TGX stain free gels (BioRad Cat. #4568095) at 200 V for 40 minutes. .. Proteins 695 were transferred to a nitrocellulose membrane using a BioRad Transblot Turbo Transfer 696 System with the MixedMW setting (25 V, 1.3 A, 7 minutes) before blocking using 1:5 697 BioRad EveryBlot Blocking Buffer (BioRad Cat. #12010020): PBS for 30 minutes at room 698 temperature. ..



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    (A) Representative Western Blots of Aβ and IDE in neuronal cells after <t>APP</t> transfection. (B) sPIF reduces Aβ formation in IDE dependent manner. (C) Identified regions of structural similarity within the set of protein structures by STRALCP. Clustering of structurally conserved fragments ( left ). STRALCP identified structural similarity between selected “ reference ” structure and other analyzed structures, represented as colored bars, based on C alpha - C alpha distance deviation at each position between the reference (top bar) and other structures ( right ). The colors indicate RMSD between aligned residues, ranging from green (below 2Å), yellow (below 4Å), orange (below 6Å), to red (above 6Å). STRALCP: STRucture ALignment-based Clustering of Proteins; RMSD: Room mean square distances; Aβ: Amyloid Beta; IDE: Insulin degrading enzyme; APP: <t>Amyloid</t> <t>precursor</t> protein; sPIF: synthetic PreImplantation Factor; * p<0.05; ** p<0.01; *** p<0.001 (ANOVA followed by two tail t test). In-vitro experiment results represent at least three independent experiments.
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    Image Search Results


    (A) Representative Western Blots of Aβ and IDE in neuronal cells after APP transfection. (B) sPIF reduces Aβ formation in IDE dependent manner. (C) Identified regions of structural similarity within the set of protein structures by STRALCP. Clustering of structurally conserved fragments ( left ). STRALCP identified structural similarity between selected “ reference ” structure and other analyzed structures, represented as colored bars, based on C alpha - C alpha distance deviation at each position between the reference (top bar) and other structures ( right ). The colors indicate RMSD between aligned residues, ranging from green (below 2Å), yellow (below 4Å), orange (below 6Å), to red (above 6Å). STRALCP: STRucture ALignment-based Clustering of Proteins; RMSD: Room mean square distances; Aβ: Amyloid Beta; IDE: Insulin degrading enzyme; APP: Amyloid precursor protein; sPIF: synthetic PreImplantation Factor; * p<0.05; ** p<0.01; *** p<0.001 (ANOVA followed by two tail t test). In-vitro experiment results represent at least three independent experiments.

    Journal: Oncotarget

    Article Title: The core sequence of PIF competes for insulin/amyloid β in insulin degrading enzyme: potential treatment for Alzheimer's disease

    doi: 10.18632/oncotarget.26057

    Figure Lengend Snippet: (A) Representative Western Blots of Aβ and IDE in neuronal cells after APP transfection. (B) sPIF reduces Aβ formation in IDE dependent manner. (C) Identified regions of structural similarity within the set of protein structures by STRALCP. Clustering of structurally conserved fragments ( left ). STRALCP identified structural similarity between selected “ reference ” structure and other analyzed structures, represented as colored bars, based on C alpha - C alpha distance deviation at each position between the reference (top bar) and other structures ( right ). The colors indicate RMSD between aligned residues, ranging from green (below 2Å), yellow (below 4Å), orange (below 6Å), to red (above 6Å). STRALCP: STRucture ALignment-based Clustering of Proteins; RMSD: Room mean square distances; Aβ: Amyloid Beta; IDE: Insulin degrading enzyme; APP: Amyloid precursor protein; sPIF: synthetic PreImplantation Factor; * p<0.05; ** p<0.01; *** p<0.001 (ANOVA followed by two tail t test). In-vitro experiment results represent at least three independent experiments.

    Article Snippet: We purchased plasmids containing amyloid precursor protein (APP) from Addgene (pCAX APP 695 #30137).

    Techniques: Western Blot, Transfection, In Vitro