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herein referred to as fgf23  (R&D Systems)


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    R&D Systems herein referred to as fgf23
    RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. ( A ) Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants (1- – 4). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 ( R1, R2 ), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. ( B ) Transfected WT-RGS14 and truncation mutants (constructs 1–4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. ( C ) Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100 nM <t>FGF23</t> or PTH before phosphate uptake measurements. n = 6. **** P < 0.001 vs . control.
    Herein Referred To As Fgf23, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/herein+referred+to+as+fgf23/pmc12133299-155-6-22?v=R%26D+Systems
    Average 94 stars, based on 40 article reviews
    herein referred to as fgf23 - by Bioz Stars, 2026-08
    94/100 stars

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    1) Product Images from "Noncanonical RGS14 structural determinants control hormone-sensitive NPT2A-mediated phosphate transport"

    Article Title: Noncanonical RGS14 structural determinants control hormone-sensitive NPT2A-mediated phosphate transport

    Journal: Biochemical Journal

    doi: 10.1042/BCJ20240122

    RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. ( A ) Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants (1- – 4). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 ( R1, R2 ), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. ( B ) Transfected WT-RGS14 and truncation mutants (constructs 1–4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. ( C ) Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100 nM FGF23 or PTH before phosphate uptake measurements. n = 6. **** P < 0.001 vs . control.
    Figure Legend Snippet: RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. ( A ) Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants (1- – 4). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 ( R1, R2 ), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. ( B ) Transfected WT-RGS14 and truncation mutants (constructs 1–4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. ( C ) Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100 nM FGF23 or PTH before phosphate uptake measurements. n = 6. **** P < 0.001 vs . control.

    Techniques Used: Generated, Functional Assay, Binding Assay, Transfection, Construct, Molecular Weight, Plasmid Preparation, Negative Control, Mutagenesis, Control

    As indicated, OK cells were seeded on 12-well plates and transfected with RGS14 (WT or mutants) or empty vector (-). Cells were treated with 100 nM FGF23 or PTH for 2 hr, and Pi uptake was measured as detailed in Experimental procedures. Data were normalized to vector control (100%). ** P < 0.01 vs . control, *** P < 0.001 vs . control, **** P < 0.0001 vs control. n = 4.
    Figure Legend Snippet: As indicated, OK cells were seeded on 12-well plates and transfected with RGS14 (WT or mutants) or empty vector (-). Cells were treated with 100 nM FGF23 or PTH for 2 hr, and Pi uptake was measured as detailed in Experimental procedures. Data were normalized to vector control (100%). ** P < 0.01 vs . control, *** P < 0.001 vs . control, **** P < 0.0001 vs control. n = 4.

    Techniques Used: Transfection, Plasmid Preparation, Control

    ( A ) RGS14 Ser 266 Ala and Ser 269 Ala phosphorylation. HPCT cells expressing the indicated HA-RGS14 linker were treated with 100 nM PTH or FGF23 for 30 min or vehicle control ( C ). Cell lysates were prepared, and the linker peptide was immunoprecipitated with anti-HA agarose (Methods). The phosphorylated linker was assessed with an anti-phosphoserine antibody. Cell lysates exhibited comparable probe expression. Molecular weight markers (kDa) are shown on the right. Illustrative of n = 4. ( B ) Paired analysis of PTH and FGF23 effects on phosphorylation of the wild-typeWT linker peptide or the mutated Ser 266,269 Ala probe. ** P < 0.01. ( C ) Hormone-induced phosphorylation of full-length RGS14. HK-2 cells were transfected with FLAG-RGS14 and HA-NHERF1. After 24 h, cells were serum-starved overnight and then treated with 100 nM FGF23 or PTH for 30 min. FLAG-RGS14 was immunoprecipitated as detailed in Experimentalexperimental Proceduresprocedures. Molecular weight markers are shown to the right. Representative of n = 6. ( D ) Quantification of hormone-stimulated phosphorylation of full-length RGS14. ** P < 0.01. ( E ) PTH and FGF23 failed to promote phosphorylation in HK-2 cells transfected with FLAG-RGS14 but not HA-NHERF1.
    Figure Legend Snippet: ( A ) RGS14 Ser 266 Ala and Ser 269 Ala phosphorylation. HPCT cells expressing the indicated HA-RGS14 linker were treated with 100 nM PTH or FGF23 for 30 min or vehicle control ( C ). Cell lysates were prepared, and the linker peptide was immunoprecipitated with anti-HA agarose (Methods). The phosphorylated linker was assessed with an anti-phosphoserine antibody. Cell lysates exhibited comparable probe expression. Molecular weight markers (kDa) are shown on the right. Illustrative of n = 4. ( B ) Paired analysis of PTH and FGF23 effects on phosphorylation of the wild-typeWT linker peptide or the mutated Ser 266,269 Ala probe. ** P < 0.01. ( C ) Hormone-induced phosphorylation of full-length RGS14. HK-2 cells were transfected with FLAG-RGS14 and HA-NHERF1. After 24 h, cells were serum-starved overnight and then treated with 100 nM FGF23 or PTH for 30 min. FLAG-RGS14 was immunoprecipitated as detailed in Experimentalexperimental Proceduresprocedures. Molecular weight markers are shown to the right. Representative of n = 6. ( D ) Quantification of hormone-stimulated phosphorylation of full-length RGS14. ** P < 0.01. ( E ) PTH and FGF23 failed to promote phosphorylation in HK-2 cells transfected with FLAG-RGS14 but not HA-NHERF1.

    Techniques Used: Phospho-proteomics, Expressing, Control, Immunoprecipitation, Molecular Weight, Transfection

    Working model of the role of RGS14 in controlling NPT2A-mediated phosphate uptake under resting conditions ( A ) and following stimulation with PTH or FGF23 ( B ). ( A ) NPT2A binds NHERF1 PDZ1 and human RGS14 binds PDZ2, stabilizing the [NHERF1:NPT2A] complex at the membrane surface permitting constitutive phosphate uptake. ( B ) PTH, acting through the PTH receptor (PTHR) or FGF23 through FGFR1, promotes RGS14 phosphorylation and its dissociation from NHERF1 leading to sequestration of NPT2A and cessation of phosphate uptake [ , ].
    Figure Legend Snippet: Working model of the role of RGS14 in controlling NPT2A-mediated phosphate uptake under resting conditions ( A ) and following stimulation with PTH or FGF23 ( B ). ( A ) NPT2A binds NHERF1 PDZ1 and human RGS14 binds PDZ2, stabilizing the [NHERF1:NPT2A] complex at the membrane surface permitting constitutive phosphate uptake. ( B ) PTH, acting through the PTH receptor (PTHR) or FGF23 through FGFR1, promotes RGS14 phosphorylation and its dissociation from NHERF1 leading to sequestration of NPT2A and cessation of phosphate uptake [ , ].

    Techniques Used: Membrane, Phospho-proteomics



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    RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. ( A ) Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants (1- – 4). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 ( R1, R2 ), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. ( B ) Transfected WT-RGS14 and truncation mutants (constructs 1–4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. ( C ) Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100 nM <t>FGF23</t> or PTH before phosphate uptake measurements. n = 6. **** P < 0.001 vs . control.
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    RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. A . Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental Procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants ( - ). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 (R1, R2), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. B . Transfected WT-RGS14 and truncation mutants (constructs1-4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. C . Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100nM <t>FGF23</t> or PTH before phosphate uptake measurements. n =6. ****p<0.001 vs control.
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    RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. ( A ) Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants (1- – 4). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 ( R1, R2 ), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. ( B ) Transfected WT-RGS14 and truncation mutants (constructs 1–4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. ( C ) Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100 nM FGF23 or PTH before phosphate uptake measurements. n = 6. **** P < 0.001 vs . control.

    Journal: Biochemical Journal

    Article Title: Noncanonical RGS14 structural determinants control hormone-sensitive NPT2A-mediated phosphate transport

    doi: 10.1042/BCJ20240122

    Figure Lengend Snippet: RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. ( A ) Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants (1- – 4). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 ( R1, R2 ), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. ( B ) Transfected WT-RGS14 and truncation mutants (constructs 1–4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. ( C ) Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100 nM FGF23 or PTH before phosphate uptake measurements. n = 6. **** P < 0.001 vs . control.

    Article Snippet: Recombinant human Arg 179 Gln-FGF23 25-251 (herein referred to as FGF23), which is resistant to furin cleavage and inactivation, was obtained from R&D Systems (2604-FG-025).

    Techniques: Generated, Functional Assay, Binding Assay, Transfection, Construct, Molecular Weight, Plasmid Preparation, Negative Control, Mutagenesis, Control

    As indicated, OK cells were seeded on 12-well plates and transfected with RGS14 (WT or mutants) or empty vector (-). Cells were treated with 100 nM FGF23 or PTH for 2 hr, and Pi uptake was measured as detailed in Experimental procedures. Data were normalized to vector control (100%). ** P < 0.01 vs . control, *** P < 0.001 vs . control, **** P < 0.0001 vs control. n = 4.

    Journal: Biochemical Journal

    Article Title: Noncanonical RGS14 structural determinants control hormone-sensitive NPT2A-mediated phosphate transport

    doi: 10.1042/BCJ20240122

    Figure Lengend Snippet: As indicated, OK cells were seeded on 12-well plates and transfected with RGS14 (WT or mutants) or empty vector (-). Cells were treated with 100 nM FGF23 or PTH for 2 hr, and Pi uptake was measured as detailed in Experimental procedures. Data were normalized to vector control (100%). ** P < 0.01 vs . control, *** P < 0.001 vs . control, **** P < 0.0001 vs control. n = 4.

    Article Snippet: Recombinant human Arg 179 Gln-FGF23 25-251 (herein referred to as FGF23), which is resistant to furin cleavage and inactivation, was obtained from R&D Systems (2604-FG-025).

    Techniques: Transfection, Plasmid Preparation, Control

    ( A ) RGS14 Ser 266 Ala and Ser 269 Ala phosphorylation. HPCT cells expressing the indicated HA-RGS14 linker were treated with 100 nM PTH or FGF23 for 30 min or vehicle control ( C ). Cell lysates were prepared, and the linker peptide was immunoprecipitated with anti-HA agarose (Methods). The phosphorylated linker was assessed with an anti-phosphoserine antibody. Cell lysates exhibited comparable probe expression. Molecular weight markers (kDa) are shown on the right. Illustrative of n = 4. ( B ) Paired analysis of PTH and FGF23 effects on phosphorylation of the wild-typeWT linker peptide or the mutated Ser 266,269 Ala probe. ** P < 0.01. ( C ) Hormone-induced phosphorylation of full-length RGS14. HK-2 cells were transfected with FLAG-RGS14 and HA-NHERF1. After 24 h, cells were serum-starved overnight and then treated with 100 nM FGF23 or PTH for 30 min. FLAG-RGS14 was immunoprecipitated as detailed in Experimentalexperimental Proceduresprocedures. Molecular weight markers are shown to the right. Representative of n = 6. ( D ) Quantification of hormone-stimulated phosphorylation of full-length RGS14. ** P < 0.01. ( E ) PTH and FGF23 failed to promote phosphorylation in HK-2 cells transfected with FLAG-RGS14 but not HA-NHERF1.

    Journal: Biochemical Journal

    Article Title: Noncanonical RGS14 structural determinants control hormone-sensitive NPT2A-mediated phosphate transport

    doi: 10.1042/BCJ20240122

    Figure Lengend Snippet: ( A ) RGS14 Ser 266 Ala and Ser 269 Ala phosphorylation. HPCT cells expressing the indicated HA-RGS14 linker were treated with 100 nM PTH or FGF23 for 30 min or vehicle control ( C ). Cell lysates were prepared, and the linker peptide was immunoprecipitated with anti-HA agarose (Methods). The phosphorylated linker was assessed with an anti-phosphoserine antibody. Cell lysates exhibited comparable probe expression. Molecular weight markers (kDa) are shown on the right. Illustrative of n = 4. ( B ) Paired analysis of PTH and FGF23 effects on phosphorylation of the wild-typeWT linker peptide or the mutated Ser 266,269 Ala probe. ** P < 0.01. ( C ) Hormone-induced phosphorylation of full-length RGS14. HK-2 cells were transfected with FLAG-RGS14 and HA-NHERF1. After 24 h, cells were serum-starved overnight and then treated with 100 nM FGF23 or PTH for 30 min. FLAG-RGS14 was immunoprecipitated as detailed in Experimentalexperimental Proceduresprocedures. Molecular weight markers are shown to the right. Representative of n = 6. ( D ) Quantification of hormone-stimulated phosphorylation of full-length RGS14. ** P < 0.01. ( E ) PTH and FGF23 failed to promote phosphorylation in HK-2 cells transfected with FLAG-RGS14 but not HA-NHERF1.

    Article Snippet: Recombinant human Arg 179 Gln-FGF23 25-251 (herein referred to as FGF23), which is resistant to furin cleavage and inactivation, was obtained from R&D Systems (2604-FG-025).

    Techniques: Phospho-proteomics, Expressing, Control, Immunoprecipitation, Molecular Weight, Transfection

    Working model of the role of RGS14 in controlling NPT2A-mediated phosphate uptake under resting conditions ( A ) and following stimulation with PTH or FGF23 ( B ). ( A ) NPT2A binds NHERF1 PDZ1 and human RGS14 binds PDZ2, stabilizing the [NHERF1:NPT2A] complex at the membrane surface permitting constitutive phosphate uptake. ( B ) PTH, acting through the PTH receptor (PTHR) or FGF23 through FGFR1, promotes RGS14 phosphorylation and its dissociation from NHERF1 leading to sequestration of NPT2A and cessation of phosphate uptake [ , ].

    Journal: Biochemical Journal

    Article Title: Noncanonical RGS14 structural determinants control hormone-sensitive NPT2A-mediated phosphate transport

    doi: 10.1042/BCJ20240122

    Figure Lengend Snippet: Working model of the role of RGS14 in controlling NPT2A-mediated phosphate uptake under resting conditions ( A ) and following stimulation with PTH or FGF23 ( B ). ( A ) NPT2A binds NHERF1 PDZ1 and human RGS14 binds PDZ2, stabilizing the [NHERF1:NPT2A] complex at the membrane surface permitting constitutive phosphate uptake. ( B ) PTH, acting through the PTH receptor (PTHR) or FGF23 through FGFR1, promotes RGS14 phosphorylation and its dissociation from NHERF1 leading to sequestration of NPT2A and cessation of phosphate uptake [ , ].

    Article Snippet: Recombinant human Arg 179 Gln-FGF23 25-251 (herein referred to as FGF23), which is resistant to furin cleavage and inactivation, was obtained from R&D Systems (2604-FG-025).

    Techniques: Membrane, Phospho-proteomics

    RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. A . Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental Procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants ( - ). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 (R1, R2), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. B . Transfected WT-RGS14 and truncation mutants (constructs1-4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. C . Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100nM FGF23 or PTH before phosphate uptake measurements. n =6. ****p<0.001 vs control.

    Journal: bioRxiv

    Article Title: Structural factors of RGS14 regulating hormone-dependent phosphate transport mediated by NPT2A

    doi: 10.1101/2024.03.29.586499

    Figure Lengend Snippet: RGS14 truncation mutants were generated to identify functional domains suppressing hormone-regulated phosphate transport. A . Serial deletions from the N-terminus of RGS14 were generated, as outlined in Experimental Procedures. Previously characterized functional domains are depicted in the full-length (WT) RGS14 and the truncation mutants ( - ). Regulator of G protein Signaling (RGS) domain, Ras-binding domains 1 and 2 (R1, R2), G protein regulatory (Go-Loco) motif, and -DSAL PDZ ligand are depicted. B . Transfected WT-RGS14 and truncation mutants (constructs1-4) expressed in HEK293 cells. Molecular weight markers (kDa) are presented for reference. Empty vector-transfected cell lysate (V) served as a negative control. C . Hormone-sensitive phosphate uptake was measured in OK cells transfected with WT-RGS14 or the indicated truncation mutant. Phosphate transport was normalized to baseline phosphate uptake under control conditions (100%). Where indicated, cells were treated with 100nM FGF23 or PTH before phosphate uptake measurements. n =6. ****p<0.001 vs control.

    Article Snippet: Recombinant human Arg 179 Gln-FGF23 25-251 (herein referred to as FGF23), which is resistant to furin cleavage and inactivation, was obtained from R&D Systems (2604-FG-025).

    Techniques: Generated, Functional Assay, Binding Assay, Transfection, Molecular Weight, Plasmid Preparation, Negative Control, Mutagenesis