bdnf pro domain  (Alomone Labs)


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    Structured Review

    Alomone Labs bdnf pro domain
    Mutational binding analysis of <t>HisS-pro-BDNF</t> to short sortilin fragments. A , <t>HisS-BDNFpro</t> binding analysis to peptides with the wild-type sortilin sequences 163 RIFRSSDF 170 and 170 FAKNFVQTD 178 listed to the left on each membrane. Binding to mutant peptides
    Bdnf Pro Domain, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bdnf pro domain/product/Alomone Labs
    Average 93 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    bdnf pro domain - by Bioz Stars, 2022-10
    93/100 stars

    Images

    1) Product Images from "Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *"

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M109.062364

    Mutational binding analysis of HisS-pro-BDNF to short sortilin fragments. A , HisS-BDNFpro binding analysis to peptides with the wild-type sortilin sequences 163 RIFRSSDF 170 and 170 FAKNFVQTD 178 listed to the left on each membrane. Binding to mutant peptides
    Figure Legend Snippet: Mutational binding analysis of HisS-pro-BDNF to short sortilin fragments. A , HisS-BDNFpro binding analysis to peptides with the wild-type sortilin sequences 163 RIFRSSDF 170 and 170 FAKNFVQTD 178 listed to the left on each membrane. Binding to mutant peptides

    Techniques Used: Binding Assay, Mutagenesis

    2) Product Images from "Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *"

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M109.062364

    Analysis of the NGF and the BDNF pro-domain binding to the mammalian VPS10p receptors by SPOT analysis. A peptide library containing a total of 2181 peptides represented by 734 from sorLA, 403 from sorCS3, 389 from sorCS1, 382 from sorCS2, and 273 from
    Figure Legend Snippet: Analysis of the NGF and the BDNF pro-domain binding to the mammalian VPS10p receptors by SPOT analysis. A peptide library containing a total of 2181 peptides represented by 734 from sorLA, 403 from sorCS3, 389 from sorCS1, 382 from sorCS2, and 273 from

    Techniques Used: Binding Assay

    Selective competition of ligands by sortilin-derived peptide antagonist. SPR binding analysis of 50 n m unprocessed pro-BDNF ( A ), 50 n m unprocessed pro-NGF ( B ), and 90 n m RAP ( C ) to immobilized sortilin in the absence and presence of the sort166–181
    Figure Legend Snippet: Selective competition of ligands by sortilin-derived peptide antagonist. SPR binding analysis of 50 n m unprocessed pro-BDNF ( A ), 50 n m unprocessed pro-NGF ( B ), and 90 n m RAP ( C ) to immobilized sortilin in the absence and presence of the sort166–181

    Techniques Used: Derivative Assay, SPR Assay, Binding Assay

    Mutation of the linear binding site specifically impairs binding of both the NGF and the BDNF pro-domains. SPR analysis showing reduced binding of equal amounts (analyte concentration: 200 n m ) of the soluble extracellular domains of sortilin-4A compared
    Figure Legend Snippet: Mutation of the linear binding site specifically impairs binding of both the NGF and the BDNF pro-domains. SPR analysis showing reduced binding of equal amounts (analyte concentration: 200 n m ) of the soluble extracellular domains of sortilin-4A compared

    Techniques Used: Mutagenesis, Binding Assay, SPR Assay, Concentration Assay

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    Alomone Labs bdnf pro domain
    Mutational binding analysis of <t>HisS-pro-BDNF</t> to short sortilin fragments. A , <t>HisS-BDNFpro</t> binding analysis to peptides with the wild-type sortilin sequences 163 RIFRSSDF 170 and 170 FAKNFVQTD 178 listed to the left on each membrane. Binding to mutant peptides
    Bdnf Pro Domain, 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/bdnf pro domain/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bdnf pro domain - by Bioz Stars, 2022-10
    93/100 stars
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    Mutational binding analysis of HisS-pro-BDNF to short sortilin fragments. A , HisS-BDNFpro binding analysis to peptides with the wild-type sortilin sequences 163 RIFRSSDF 170 and 170 FAKNFVQTD 178 listed to the left on each membrane. Binding to mutant peptides

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    doi: 10.1074/jbc.M109.062364

    Figure Lengend Snippet: Mutational binding analysis of HisS-pro-BDNF to short sortilin fragments. A , HisS-BDNFpro binding analysis to peptides with the wild-type sortilin sequences 163 RIFRSSDF 170 and 170 FAKNFVQTD 178 listed to the left on each membrane. Binding to mutant peptides

    Article Snippet: Second, this interaction critically depended on the surface-exposed amino acids Arg163 , Phe165 , and Arg166 for both NGFpro and BDNFpro, whereas Phe170 and Phe174 also contributed to the binding of the BDNF pro-domain, an observation that may explain the higher affinity of sortilin for pro-BDNF than pro-NGF ( D and ) ( , ).

    Techniques: Binding Assay, Mutagenesis

    Analysis of the NGF and the BDNF pro-domain binding to the mammalian VPS10p receptors by SPOT analysis. A peptide library containing a total of 2181 peptides represented by 734 from sorLA, 403 from sorCS3, 389 from sorCS1, 382 from sorCS2, and 273 from

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    doi: 10.1074/jbc.M109.062364

    Figure Lengend Snippet: Analysis of the NGF and the BDNF pro-domain binding to the mammalian VPS10p receptors by SPOT analysis. A peptide library containing a total of 2181 peptides represented by 734 from sorLA, 403 from sorCS3, 389 from sorCS1, 382 from sorCS2, and 273 from

    Article Snippet: We found that the higher affinity of the BDNF pro-domain as compared with the NGF pro-domain for sortilin ( and Refs. , ) could be replicated when using the sortilin peptide.

    Techniques: Binding Assay

    Selective competition of ligands by sortilin-derived peptide antagonist. SPR binding analysis of 50 n m unprocessed pro-BDNF ( A ), 50 n m unprocessed pro-NGF ( B ), and 90 n m RAP ( C ) to immobilized sortilin in the absence and presence of the sort166–181

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    doi: 10.1074/jbc.M109.062364

    Figure Lengend Snippet: Selective competition of ligands by sortilin-derived peptide antagonist. SPR binding analysis of 50 n m unprocessed pro-BDNF ( A ), 50 n m unprocessed pro-NGF ( B ), and 90 n m RAP ( C ) to immobilized sortilin in the absence and presence of the sort166–181

    Article Snippet: We found that the higher affinity of the BDNF pro-domain as compared with the NGF pro-domain for sortilin ( and Refs. , ) could be replicated when using the sortilin peptide.

    Techniques: Derivative Assay, SPR Assay, Binding Assay

    Mutation of the linear binding site specifically impairs binding of both the NGF and the BDNF pro-domains. SPR analysis showing reduced binding of equal amounts (analyte concentration: 200 n m ) of the soluble extracellular domains of sortilin-4A compared

    Journal: The Journal of Biological Chemistry

    Article Title: Identification of a Linear Epitope in Sortilin That Partakes in Pro-neurotrophin Binding *

    doi: 10.1074/jbc.M109.062364

    Figure Lengend Snippet: Mutation of the linear binding site specifically impairs binding of both the NGF and the BDNF pro-domains. SPR analysis showing reduced binding of equal amounts (analyte concentration: 200 n m ) of the soluble extracellular domains of sortilin-4A compared

    Article Snippet: We found that the higher affinity of the BDNF pro-domain as compared with the NGF pro-domain for sortilin ( and Refs. , ) could be replicated when using the sortilin peptide.

    Techniques: Mutagenesis, Binding Assay, SPR Assay, Concentration Assay