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human fgfr1c  (R&D Systems)


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    R&D Systems human fgfr1c
    Human Fgfr1c, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human fgfr1c/product/R&D Systems
    Average 93 stars, based on 10 article reviews
    human fgfr1c - by Bioz Stars, 2026-02
    93/100 stars

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    Site mutagenesis and structural modeling analysis further indicated that N-glycans might directly modulate Klotho's protein folding and co-receptor function. A, a single N-linked site mutant of sKlotho was transiently transfected into HEK293 cells as described under “Experimental procedures.” Both conditioned medium (CM) and cell pellets were analyzed by SDS-PAGE and immunoblotted with anti-His4 antibody (Qiagen, Germantown, MD). B, structural modeling of <t>sKlotho/FGFR1c/FGF23</t> complex. Structure from Protein Data Bank entry 5W21 (32) was modeled with extended sugar chains from Fc glycan in Protein Data Bank entry 5VGP.
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    Site mutagenesis and structural modeling analysis further indicated that N-glycans might directly modulate Klotho's protein folding and co-receptor function. A, a single N-linked site mutant of sKlotho was transiently transfected into HEK293 cells as described under “Experimental procedures.” Both conditioned medium (CM) and cell pellets were analyzed by SDS-PAGE and immunoblotted with anti-His4 antibody (Qiagen, Germantown, MD). B, structural modeling of <t>sKlotho/FGFR1c/FGF23</t> complex. Structure from Protein Data Bank entry 5W21 (32) was modeled with extended sugar chains from Fc glycan in Protein Data Bank entry 5VGP.
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    Site mutagenesis and structural modeling analysis further indicated that N-glycans might directly modulate Klotho's protein folding and co-receptor function. A, a single N-linked site mutant of sKlotho was transiently transfected into HEK293 cells as described under “Experimental procedures.” Both conditioned medium (CM) and cell pellets were analyzed by SDS-PAGE and immunoblotted with anti-His4 antibody (Qiagen, Germantown, MD). B, structural modeling of sKlotho/FGFR1c/FGF23 complex. Structure from Protein Data Bank entry 5W21 (32) was modeled with extended sugar chains from Fc glycan in Protein Data Bank entry 5VGP.

    Journal: The Journal of Biological Chemistry

    Article Title: Structure-function relationships of the soluble form of the antiaging protein Klotho have therapeutic implications for managing kidney disease

    doi: 10.1074/jbc.RA119.012144

    Figure Lengend Snippet: Site mutagenesis and structural modeling analysis further indicated that N-glycans might directly modulate Klotho's protein folding and co-receptor function. A, a single N-linked site mutant of sKlotho was transiently transfected into HEK293 cells as described under “Experimental procedures.” Both conditioned medium (CM) and cell pellets were analyzed by SDS-PAGE and immunoblotted with anti-His4 antibody (Qiagen, Germantown, MD). B, structural modeling of sKlotho/FGFR1c/FGF23 complex. Structure from Protein Data Bank entry 5W21 (32) was modeled with extended sugar chains from Fc glycan in Protein Data Bank entry 5VGP.

    Article Snippet: Stably transfected L6 cells expressing human FGFR1c (Biomiga, Inc., San Diego, CA) were maintained in RPMI medium containing 10% FBS and 7 μg/ml puromycin.

    Techniques: Mutagenesis, Transfection, SDS Page, Glycoproteomics

    Site mutagenesis and structural modeling analysis further indicated that N-glycans might directly modulate Klotho's protein folding and co-receptor function. A, a single N-linked site mutant of sKlotho was transiently transfected into HEK293 cells as described under “Experimental procedures.” Both conditioned medium (CM) and cell pellets were analyzed by SDS-PAGE and immunoblotted with anti-His4 antibody (Qiagen, Germantown, MD). B, structural modeling of sKlotho/FGFR1c/FGF23 complex. Structure from Protein Data Bank entry 5W21 (32) was modeled with extended sugar chains from Fc glycan in Protein Data Bank entry 5VGP.

    Journal: The Journal of Biological Chemistry

    Article Title: Structure-function relationships of the soluble form of the antiaging protein Klotho have therapeutic implications for managing kidney disease

    doi: 10.1074/jbc.RA119.012144

    Figure Lengend Snippet: Site mutagenesis and structural modeling analysis further indicated that N-glycans might directly modulate Klotho's protein folding and co-receptor function. A, a single N-linked site mutant of sKlotho was transiently transfected into HEK293 cells as described under “Experimental procedures.” Both conditioned medium (CM) and cell pellets were analyzed by SDS-PAGE and immunoblotted with anti-His4 antibody (Qiagen, Germantown, MD). B, structural modeling of sKlotho/FGFR1c/FGF23 complex. Structure from Protein Data Bank entry 5W21 (32) was modeled with extended sugar chains from Fc glycan in Protein Data Bank entry 5VGP.

    Article Snippet: ERK1/2 activation assay Stably transfected L6 cells expressing human FGFR1c (Biomiga, Inc., San Diego, CA) were maintained in RPMI medium containing 10% FBS and 7 μg/ml puromycin.

    Techniques: Mutagenesis, Transfection, SDS Page, Glycoproteomics