ig1 domain Search Results


ig1-3-a + b + (aa 30d-318l)  (Becton Dickinson)
90
Becton Dickinson ig1-3-a + b + (aa 30d-318l)
( a–c ) Coprecipitation between recombinant ectodomains of SALM5 and LAR. LAR ectodomain proteins (LAR-Ecto-Fc or LAR-IgFN14-Fc <t>[Ig1-3</t> + FN1-4]) and HA-SALM5-Ecto secreted from transfected HEK293T cells into the supernatant were subjected to immunoprecipitation (IP) and immunoblot analysis. ( d–g ) Direct interaction between purified, soluble LAR and SALM5 fusion proteins, measured by the biolayer interferometry. Hybrid SALM5-Ecto proteins binds LAR-Ig-FN12 and LAR-Ig but not to LAR-FN12 fusion proteins ( d–f ), which is summarized in a schematic diagram ( g ). A hybrid SALM5 protein was used to increase protein expression levels (see Materials and methods for details). Note that the LAR constructs longer than the Ig domains only used here (LAR-FN12) and in the coimmunoprecipitation experiments (LAR-Ig-FN14) would not interfere with demonstrating the direction interaction of LAR with SALM5, as evident in .
Ig1 3 A + B + (Aa 30d 318l), supplied by Becton Dickinson, 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/ig1+domain/pmc04881023-121-5-22?v=Becton+Dickinson
Average 90 stars, based on 1 article reviews
ig1-3-a + b + (aa 30d-318l) - by Bioz Stars, 2026-07
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( a–c ) Coprecipitation between recombinant ectodomains of SALM5 and LAR. LAR ectodomain proteins (LAR-Ecto-Fc or LAR-IgFN14-Fc [Ig1-3 + FN1-4]) and HA-SALM5-Ecto secreted from transfected HEK293T cells into the supernatant were subjected to immunoprecipitation (IP) and immunoblot analysis. ( d–g ) Direct interaction between purified, soluble LAR and SALM5 fusion proteins, measured by the biolayer interferometry. Hybrid SALM5-Ecto proteins binds LAR-Ig-FN12 and LAR-Ig but not to LAR-FN12 fusion proteins ( d–f ), which is summarized in a schematic diagram ( g ). A hybrid SALM5 protein was used to increase protein expression levels (see Materials and methods for details). Note that the LAR constructs longer than the Ig domains only used here (LAR-FN12) and in the coimmunoprecipitation experiments (LAR-Ig-FN14) would not interfere with demonstrating the direction interaction of LAR with SALM5, as evident in .

Journal: Scientific Reports

Article Title: SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development

doi: 10.1038/srep26676

Figure Lengend Snippet: ( a–c ) Coprecipitation between recombinant ectodomains of SALM5 and LAR. LAR ectodomain proteins (LAR-Ecto-Fc or LAR-IgFN14-Fc [Ig1-3 + FN1-4]) and HA-SALM5-Ecto secreted from transfected HEK293T cells into the supernatant were subjected to immunoprecipitation (IP) and immunoblot analysis. ( d–g ) Direct interaction between purified, soluble LAR and SALM5 fusion proteins, measured by the biolayer interferometry. Hybrid SALM5-Ecto proteins binds LAR-Ig-FN12 and LAR-Ig but not to LAR-FN12 fusion proteins ( d–f ), which is summarized in a schematic diagram ( g ). A hybrid SALM5 protein was used to increase protein expression levels (see Materials and methods for details). Note that the LAR constructs longer than the Ig domains only used here (LAR-FN12) and in the coimmunoprecipitation experiments (LAR-Ig-FN14) would not interfere with demonstrating the direction interaction of LAR with SALM5, as evident in .

Article Snippet: The Ig1-3-FNIII12 domain (aa 27A–513A), Ig1-3-A + B + (aa 30D-318L), and FN12 (aa 312Q–510G) of human LAR were cloned into pAcGP67 (BD Bioscience), modified for C-terminal protein-A tagging.

Techniques: Recombinant, Transfection, Immunoprecipitation, Western Blot, Purification, Expressing, Construct