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peptide spots blot  (Jerini Inc)

 
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    Jerini Inc peptide spots blot
    Fine mapping of cTnT residues interacting <t>with</t> <t>PKA-R.</t> The 288-amino acid residues of human cTnT were displayed on a <t>SPOTS</t> blot membrane as a series of 139 overlapping 13-mer peptides frameshifted by two residues. The cTnT SPOTS blot was tested for interaction with PKA-RII in a solid phase assay (in the presence of 20 μm Ht31 or Ht31P). PKA-RII has the highest affinity for the peptides spanning amino acids 207–227, as predicted from multiple sequence alignment and Y2H data. The other spots represent nonspecific interactions. Data shown are from a single experiment and are representative of 3 separate experiments.
    Peptide Spots Blot, supplied by Jerini Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/peptide+spots+blot/peptide+spots+blot/pmc03013013-898-6-10
    Average 90 stars, based on 1 article reviews
    peptide spots blot - by Bioz Stars, 2026-09
    90/100 stars

    Images

    1) Product Images from "Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments * "

    Article Title: Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.148684

    Fine mapping of cTnT residues interacting with PKA-R. The 288-amino acid residues of human cTnT were displayed on a SPOTS blot membrane as a series of 139 overlapping 13-mer peptides frameshifted by two residues. The cTnT SPOTS blot was tested for interaction with PKA-RII in a solid phase assay (in the presence of 20 μm Ht31 or Ht31P). PKA-RII has the highest affinity for the peptides spanning amino acids 207–227, as predicted from multiple sequence alignment and Y2H data. The other spots represent nonspecific interactions. Data shown are from a single experiment and are representative of 3 separate experiments.
    Figure Legend Snippet: Fine mapping of cTnT residues interacting with PKA-R. The 288-amino acid residues of human cTnT were displayed on a SPOTS blot membrane as a series of 139 overlapping 13-mer peptides frameshifted by two residues. The cTnT SPOTS blot was tested for interaction with PKA-RII in a solid phase assay (in the presence of 20 μm Ht31 or Ht31P). PKA-RII has the highest affinity for the peptides spanning amino acids 207–227, as predicted from multiple sequence alignment and Y2H data. The other spots represent nonspecific interactions. Data shown are from a single experiment and are representative of 3 separate experiments.

    Techniques Used: Membrane, Sequencing

    Related Articles

    Binding Assay:

    Article Title: Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments
    Article Snippet: .. PKA binding residues were confirmed using peptide SPOTS blot technology (Jerini Peptide Technology). ..

    Article Title: Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments
    Article Snippet: .. 534 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME 286 • NUMBER 1 • JANUARY 7, 2011 by guest on A ugust 17, 2015 http://w w w .jbc.org/ D ow nloaded from Solid Phase Peptide Scan Binding Assays Corroborate PKA Binding Site on cTnT—PKA binding residues were confirmed using peptide SPOTS blot technology (Jerini Peptide Technology). ..



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    Image Search Results


    Fine mapping of cTnT residues interacting with PKA-R. The 288-amino acid residues of human cTnT were displayed on a SPOTS blot membrane as a series of 139 overlapping 13-mer peptides frameshifted by two residues. The cTnT SPOTS blot was tested for interaction with PKA-RII in a solid phase assay (in the presence of 20 μm Ht31 or Ht31P). PKA-RII has the highest affinity for the peptides spanning amino acids 207–227, as predicted from multiple sequence alignment and Y2H data. The other spots represent nonspecific interactions. Data shown are from a single experiment and are representative of 3 separate experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments *

    doi: 10.1074/jbc.M110.148684

    Figure Lengend Snippet: Fine mapping of cTnT residues interacting with PKA-R. The 288-amino acid residues of human cTnT were displayed on a SPOTS blot membrane as a series of 139 overlapping 13-mer peptides frameshifted by two residues. The cTnT SPOTS blot was tested for interaction with PKA-RII in a solid phase assay (in the presence of 20 μm Ht31 or Ht31P). PKA-RII has the highest affinity for the peptides spanning amino acids 207–227, as predicted from multiple sequence alignment and Y2H data. The other spots represent nonspecific interactions. Data shown are from a single experiment and are representative of 3 separate experiments.

    Article Snippet: PKA binding residues were confirmed using peptide SPOTS blot technology (Jerini Peptide Technology).

    Techniques: Membrane, Sequencing

    Fine mapping of cTnT residues interacting with PKA-R. The 288-amino acid residues of human cTnT were displayed on a SPOTS blot membrane as a series of 139 overlapping 13-mer peptides frameshifted by two residues. The cTnT SPOTS blot was tested for interaction with PKA-RII in a solid phase assay (in the presence of 20 μm Ht31 or Ht31P). PKA-RII has the highest affinity for the peptides spanning amino acids 207–227, as predicted from multiple sequence alignment and Y2H data. The other spots represent nonspecific interactions. Data shown are from a single experiment and are representative of 3 separate experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments *

    doi: 10.1074/jbc.M110.148684

    Figure Lengend Snippet: Fine mapping of cTnT residues interacting with PKA-R. The 288-amino acid residues of human cTnT were displayed on a SPOTS blot membrane as a series of 139 overlapping 13-mer peptides frameshifted by two residues. The cTnT SPOTS blot was tested for interaction with PKA-RII in a solid phase assay (in the presence of 20 μm Ht31 or Ht31P). PKA-RII has the highest affinity for the peptides spanning amino acids 207–227, as predicted from multiple sequence alignment and Y2H data. The other spots represent nonspecific interactions. Data shown are from a single experiment and are representative of 3 separate experiments.

    Article Snippet: Solid Phase Peptide Scan Binding Assays Corroborate PKA Binding Site on cTnT PKA binding residues were confirmed using peptide SPOTS blot technology (Jerini Peptide Technology).

    Techniques: Membrane, Sequencing