c terminus  (Alomone Labs)


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    Alomone Labs c terminus
    C Terminus, supplied by Alomone Labs, 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/result/c terminus/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    c terminus - by Bioz Stars, 2022-08
    93/100 stars

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    Alomone Labs kv1 5 c terminus
    Binding of the C-terminal domain of Kv to Kvβ (a)  Western blots of Kvβ2 (upper panel) and Kvβ3 (middle panel) pulled down by the GST-Kv1.5 C-terminus fusion peptides. Fusion proteins containing 60, 38, or 19 terminal amino acid peptides from Kvα1.5 C-terminus attached to GST or GST with unrelated peptide (Control; 30μ g each) were incubated with lysate of Kvβ2 or Kvβ3 -expressing  E.coli  (350 μ g total protein). Protein complexes were pulled down using GST·Bind beads, washed and eluted with 10mM glutathione. The eluate was separated by SDS-PAGE and probed with anti-pan-Kvβ antibody, an antibody directed against the C-terminus of Kv1.5 (bait) or GST;  (b)  Densitometric analysis of the bands in panel a. The density of the Kvβ band precipitated with GST-C60 was assigned a 100% value. †, P
    Kv1 5 C Terminus, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kv1 5 c terminus/product/Alomone Labs
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    kv1 5 c terminus - by Bioz Stars, 2022-08
    80/100 stars
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    Binding of the C-terminal domain of Kv to Kvβ (a)  Western blots of Kvβ2 (upper panel) and Kvβ3 (middle panel) pulled down by the GST-Kv1.5 C-terminus fusion peptides. Fusion proteins containing 60, 38, or 19 terminal amino acid peptides from Kvα1.5 C-terminus attached to GST or GST with unrelated peptide (Control; 30μ g each) were incubated with lysate of Kvβ2 or Kvβ3 -expressing  E.coli  (350 μ g total protein). Protein complexes were pulled down using GST·Bind beads, washed and eluted with 10mM glutathione. The eluate was separated by SDS-PAGE and probed with anti-pan-Kvβ antibody, an antibody directed against the C-terminus of Kv1.5 (bait) or GST;  (b)  Densitometric analysis of the bands in panel a. The density of the Kvβ band precipitated with GST-C60 was assigned a 100% value. †, P

    Journal: Pflugers Archiv

    Article Title: Interactions between the C-terminus of Kv1.5 and Kv? regulate pyridine nucleotide-dependent changes in channel gating

    doi: 10.1007/s00424-012-1093-z

    Figure Lengend Snippet: Binding of the C-terminal domain of Kv to Kvβ (a) Western blots of Kvβ2 (upper panel) and Kvβ3 (middle panel) pulled down by the GST-Kv1.5 C-terminus fusion peptides. Fusion proteins containing 60, 38, or 19 terminal amino acid peptides from Kvα1.5 C-terminus attached to GST or GST with unrelated peptide (Control; 30μ g each) were incubated with lysate of Kvβ2 or Kvβ3 -expressing E.coli (350 μ g total protein). Protein complexes were pulled down using GST·Bind beads, washed and eluted with 10mM glutathione. The eluate was separated by SDS-PAGE and probed with anti-pan-Kvβ antibody, an antibody directed against the C-terminus of Kv1.5 (bait) or GST; (b) Densitometric analysis of the bands in panel a. The density of the Kvβ band precipitated with GST-C60 was assigned a 100% value. †, P

    Article Snippet: To further examine the propensity of the C-terminal domain of Kv1.5 to bind ancillary subunits, we compared the amino acid sequence of Kv1.5 C-terminus to that of Kv1.2 and the Drosophila Shaker channel ( ).

    Techniques: Binding Assay, Western Blot, Incubation, Expressing, SDS Page