Review



recombinant human impβ  (Novus Biologicals)


Bioz Verified Symbol Novus Biologicals is a verified supplier
Bioz Manufacturer Symbol Novus Biologicals manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 93
      Buy from Supplier

    Structured Review

    Novus Biologicals recombinant human impβ
    Fig. 1. Effect of substitution of lysine residues in the Ku70 NLS with ace tyl–lysine on binding to Impα. (A) The effect of amino acid substitutions in the Ku70 NLS on Impα binding. The binding activity of Ku70 NLS and its mutant peptides to Impα in the presence of <t>Impβ</t> was analyzed by probing immunoblots with antibodies against Impα. (B) Quantification of the pull-down assays pre sented in panel (A). Measurements of the blot band intensity were performed using ImageJ 1.52a. Each graph represents the relative intensity with Ku70 NLS WT defined as 100%. The error bars indicate the standard deviation from three independent experiments. *p < 0.05 significant differences from the case when the expected value was defined as 100.
    Recombinant Human Impβ, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+imp%CE%B2/pm36620088-38-29-33?v=Novus+Biologicals
    Average 93 stars, based on 3 article reviews
    recombinant human impβ - by Bioz Stars, 2026-07
    93/100 stars

    Images

    1) Product Images from "Acetylation of the nuclear localization signal in Ku70 diminishes the interaction with importin-α."

    Article Title: Acetylation of the nuclear localization signal in Ku70 diminishes the interaction with importin-α.

    Journal: Biochemistry and biophysics reports

    doi: 10.1016/j.bbrep.2022.101418

    Fig. 1. Effect of substitution of lysine residues in the Ku70 NLS with ace tyl–lysine on binding to Impα. (A) The effect of amino acid substitutions in the Ku70 NLS on Impα binding. The binding activity of Ku70 NLS and its mutant peptides to Impα in the presence of Impβ was analyzed by probing immunoblots with antibodies against Impα. (B) Quantification of the pull-down assays pre sented in panel (A). Measurements of the blot band intensity were performed using ImageJ 1.52a. Each graph represents the relative intensity with Ku70 NLS WT defined as 100%. The error bars indicate the standard deviation from three independent experiments. *p < 0.05 significant differences from the case when the expected value was defined as 100.
    Figure Legend Snippet: Fig. 1. Effect of substitution of lysine residues in the Ku70 NLS with ace tyl–lysine on binding to Impα. (A) The effect of amino acid substitutions in the Ku70 NLS on Impα binding. The binding activity of Ku70 NLS and its mutant peptides to Impα in the presence of Impβ was analyzed by probing immunoblots with antibodies against Impα. (B) Quantification of the pull-down assays pre sented in panel (A). Measurements of the blot band intensity were performed using ImageJ 1.52a. Each graph represents the relative intensity with Ku70 NLS WT defined as 100%. The error bars indicate the standard deviation from three independent experiments. *p < 0.05 significant differences from the case when the expected value was defined as 100.

    Techniques Used: Binding Assay, Activity Assay, Mutagenesis, Western Blot, Standard Deviation



    Similar Products

    recombinant human impβ  (Novus Biologicals)
    93
    Novus Biologicals recombinant human impβ
    Fig. 1. Effect of substitution of lysine residues in the Ku70 NLS with ace tyl–lysine on binding to Impα. (A) The effect of amino acid substitutions in the Ku70 NLS on Impα binding. The binding activity of Ku70 NLS and its mutant peptides to Impα in the presence of <t>Impβ</t> was analyzed by probing immunoblots with antibodies against Impα. (B) Quantification of the pull-down assays pre sented in panel (A). Measurements of the blot band intensity were performed using ImageJ 1.52a. Each graph represents the relative intensity with Ku70 NLS WT defined as 100%. The error bars indicate the standard deviation from three independent experiments. *p < 0.05 significant differences from the case when the expected value was defined as 100.
    Recombinant Human Impβ, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+imp%CE%B2/pm36620088-38-29-33?v=Novus+Biologicals
    Average 93 stars, based on 1 article reviews
    recombinant human impβ - by Bioz Stars, 2026-07
    93/100 stars
    		  Buy from Supplier

    Image Search Results


    Fig. 1. Effect of substitution of lysine residues in the Ku70 NLS with ace tyl–lysine on binding to Impα. (A) The effect of amino acid substitutions in the Ku70 NLS on Impα binding. The binding activity of Ku70 NLS and its mutant peptides to Impα in the presence of Impβ was analyzed by probing immunoblots with antibodies against Impα. (B) Quantification of the pull-down assays pre sented in panel (A). Measurements of the blot band intensity were performed using ImageJ 1.52a. Each graph represents the relative intensity with Ku70 NLS WT defined as 100%. The error bars indicate the standard deviation from three independent experiments. *p < 0.05 significant differences from the case when the expected value was defined as 100.

    Journal: Biochemistry and biophysics reports

    Article Title: Acetylation of the nuclear localization signal in Ku70 diminishes the interaction with importin-α.

    doi: 10.1016/j.bbrep.2022.101418

    Figure Lengend Snippet: Fig. 1. Effect of substitution of lysine residues in the Ku70 NLS with ace tyl–lysine on binding to Impα. (A) The effect of amino acid substitutions in the Ku70 NLS on Impα binding. The binding activity of Ku70 NLS and its mutant peptides to Impα in the presence of Impβ was analyzed by probing immunoblots with antibodies against Impα. (B) Quantification of the pull-down assays pre sented in panel (A). Measurements of the blot band intensity were performed using ImageJ 1.52a. Each graph represents the relative intensity with Ku70 NLS WT defined as 100%. The error bars indicate the standard deviation from three independent experiments. *p < 0.05 significant differences from the case when the expected value was defined as 100.

    Article Snippet: A binding assay was performed with 50 μl NLS-immobilized sepharose, 1 mg/ml bovine serum albumin, 0.1 μg recombinant human Impα2 (NBP1-78888; Novus Biologicals, Centennial, CO, USA), and 0.1 μg recombinant human Impβ (NBP1-78815; Novus Biologicals) in 0.5 ml transport buffer by incubation for 2 h at 4 ◦C with gentle rotation.

    Techniques: Binding Assay, Activity Assay, Mutagenesis, Western Blot, Standard Deviation