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human sost protein  (MedChemExpress)


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    MedChemExpress human sost protein
    Screening and analysis of high-affinity epitopes on <t>SOST.</t> (A) ELISA experiments were conducted to identify SOST fragments with strong binding affinity for ROMO, revealing that SOST 114–143 and SOST 143–173 exhibit significantly higher affinity ( P <0.01). (B) A schematic diagram delineating the binding functional regions associated with the high-affinity fragments of SOST. (C) ELISA results indicate that SOST 131–163 displays the highest affinity for ROMO ( P <0.01), thereby identifying it as a potent functional epitope of SOST. (D-a) SOST 131–163 fragment (highlighted in yellow) is located within the loop3 domain of <t>SOST</t> <t>protein.</t> (D-b) Docking studies indicate that SOST 131–163 fragment interacts with ROMO light chain, yielding a binding free energy of -25.8 kcal/mol and an interface area of 712.9 Ų. (D-c) Additionally, SOST 131–163 fragment can bind to the ROMO heavy chain, resulting in a binding free energy of -33.19 kcal/mol and an interface area of 451.6 Ų. (E) CTL epitopes within SOST 131–163 sequence include two strong binder epitopes and four weak binder epitopes. (F) HTL epitopes in SOST 131–163 sequence comprise one strong binder epitope and four weak binder epitopes. Predictions of B cell epitopes for SOST 131–163 sequence are illustrated, including predicted linear B cell epitopes (G) and predicted discontinuous B cell epitopes (H) .
    Human Sost Protein, supplied by MedChemExpress, 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/human sost protein/product/MedChemExpress
    Average 93 stars, based on 1 article reviews
    human sost protein - by Bioz Stars, 2026-06
    93/100 stars

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    1) Product Images from "In silico design of novel precision vaccine targeting sclerostin epitopes for osteoporosis prevention and treatment"

    Article Title: In silico design of novel precision vaccine targeting sclerostin epitopes for osteoporosis prevention and treatment

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2025.1644437

    Screening and analysis of high-affinity epitopes on SOST. (A) ELISA experiments were conducted to identify SOST fragments with strong binding affinity for ROMO, revealing that SOST 114–143 and SOST 143–173 exhibit significantly higher affinity ( P <0.01). (B) A schematic diagram delineating the binding functional regions associated with the high-affinity fragments of SOST. (C) ELISA results indicate that SOST 131–163 displays the highest affinity for ROMO ( P <0.01), thereby identifying it as a potent functional epitope of SOST. (D-a) SOST 131–163 fragment (highlighted in yellow) is located within the loop3 domain of SOST protein. (D-b) Docking studies indicate that SOST 131–163 fragment interacts with ROMO light chain, yielding a binding free energy of -25.8 kcal/mol and an interface area of 712.9 Ų. (D-c) Additionally, SOST 131–163 fragment can bind to the ROMO heavy chain, resulting in a binding free energy of -33.19 kcal/mol and an interface area of 451.6 Ų. (E) CTL epitopes within SOST 131–163 sequence include two strong binder epitopes and four weak binder epitopes. (F) HTL epitopes in SOST 131–163 sequence comprise one strong binder epitope and four weak binder epitopes. Predictions of B cell epitopes for SOST 131–163 sequence are illustrated, including predicted linear B cell epitopes (G) and predicted discontinuous B cell epitopes (H) .
    Figure Legend Snippet: Screening and analysis of high-affinity epitopes on SOST. (A) ELISA experiments were conducted to identify SOST fragments with strong binding affinity for ROMO, revealing that SOST 114–143 and SOST 143–173 exhibit significantly higher affinity ( P <0.01). (B) A schematic diagram delineating the binding functional regions associated with the high-affinity fragments of SOST. (C) ELISA results indicate that SOST 131–163 displays the highest affinity for ROMO ( P <0.01), thereby identifying it as a potent functional epitope of SOST. (D-a) SOST 131–163 fragment (highlighted in yellow) is located within the loop3 domain of SOST protein. (D-b) Docking studies indicate that SOST 131–163 fragment interacts with ROMO light chain, yielding a binding free energy of -25.8 kcal/mol and an interface area of 712.9 Ų. (D-c) Additionally, SOST 131–163 fragment can bind to the ROMO heavy chain, resulting in a binding free energy of -33.19 kcal/mol and an interface area of 451.6 Ų. (E) CTL epitopes within SOST 131–163 sequence include two strong binder epitopes and four weak binder epitopes. (F) HTL epitopes in SOST 131–163 sequence comprise one strong binder epitope and four weak binder epitopes. Predictions of B cell epitopes for SOST 131–163 sequence are illustrated, including predicted linear B cell epitopes (G) and predicted discontinuous B cell epitopes (H) .

    Techniques Used: Enzyme-linked Immunosorbent Assay, Binding Assay, Functional Assay, Sequencing



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    Screening and analysis of high-affinity epitopes on <t>SOST.</t> (A) ELISA experiments were conducted to identify SOST fragments with strong binding affinity for ROMO, revealing that SOST 114–143 and SOST 143–173 exhibit significantly higher affinity ( P <0.01). (B) A schematic diagram delineating the binding functional regions associated with the high-affinity fragments of SOST. (C) ELISA results indicate that SOST 131–163 displays the highest affinity for ROMO ( P <0.01), thereby identifying it as a potent functional epitope of SOST. (D-a) SOST 131–163 fragment (highlighted in yellow) is located within the loop3 domain of <t>SOST</t> <t>protein.</t> (D-b) Docking studies indicate that SOST 131–163 fragment interacts with ROMO light chain, yielding a binding free energy of -25.8 kcal/mol and an interface area of 712.9 Ų. (D-c) Additionally, SOST 131–163 fragment can bind to the ROMO heavy chain, resulting in a binding free energy of -33.19 kcal/mol and an interface area of 451.6 Ų. (E) CTL epitopes within SOST 131–163 sequence include two strong binder epitopes and four weak binder epitopes. (F) HTL epitopes in SOST 131–163 sequence comprise one strong binder epitope and four weak binder epitopes. Predictions of B cell epitopes for SOST 131–163 sequence are illustrated, including predicted linear B cell epitopes (G) and predicted discontinuous B cell epitopes (H) .
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    Screening and analysis of high-affinity epitopes on <t>SOST.</t> (A) ELISA experiments were conducted to identify SOST fragments with strong binding affinity for ROMO, revealing that SOST 114–143 and SOST 143–173 exhibit significantly higher affinity ( P <0.01). (B) A schematic diagram delineating the binding functional regions associated with the high-affinity fragments of SOST. (C) ELISA results indicate that SOST 131–163 displays the highest affinity for ROMO ( P <0.01), thereby identifying it as a potent functional epitope of SOST. (D-a) SOST 131–163 fragment (highlighted in yellow) is located within the loop3 domain of <t>SOST</t> <t>protein.</t> (D-b) Docking studies indicate that SOST 131–163 fragment interacts with ROMO light chain, yielding a binding free energy of -25.8 kcal/mol and an interface area of 712.9 Ų. (D-c) Additionally, SOST 131–163 fragment can bind to the ROMO heavy chain, resulting in a binding free energy of -33.19 kcal/mol and an interface area of 451.6 Ų. (E) CTL epitopes within SOST 131–163 sequence include two strong binder epitopes and four weak binder epitopes. (F) HTL epitopes in SOST 131–163 sequence comprise one strong binder epitope and four weak binder epitopes. Predictions of B cell epitopes for SOST 131–163 sequence are illustrated, including predicted linear B cell epitopes (G) and predicted discontinuous B cell epitopes (H) .
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    Screening and analysis of high-affinity epitopes on <t>SOST.</t> (A) ELISA experiments were conducted to identify SOST fragments with strong binding affinity for ROMO, revealing that SOST 114–143 and SOST 143–173 exhibit significantly higher affinity ( P <0.01). (B) A schematic diagram delineating the binding functional regions associated with the high-affinity fragments of SOST. (C) ELISA results indicate that SOST 131–163 displays the highest affinity for ROMO ( P <0.01), thereby identifying it as a potent functional epitope of SOST. (D-a) SOST 131–163 fragment (highlighted in yellow) is located within the loop3 domain of <t>SOST</t> <t>protein.</t> (D-b) Docking studies indicate that SOST 131–163 fragment interacts with ROMO light chain, yielding a binding free energy of -25.8 kcal/mol and an interface area of 712.9 Ų. (D-c) Additionally, SOST 131–163 fragment can bind to the ROMO heavy chain, resulting in a binding free energy of -33.19 kcal/mol and an interface area of 451.6 Ų. (E) CTL epitopes within SOST 131–163 sequence include two strong binder epitopes and four weak binder epitopes. (F) HTL epitopes in SOST 131–163 sequence comprise one strong binder epitope and four weak binder epitopes. Predictions of B cell epitopes for SOST 131–163 sequence are illustrated, including predicted linear B cell epitopes (G) and predicted discontinuous B cell epitopes (H) .
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    Screening and analysis of high-affinity epitopes on SOST. (A) ELISA experiments were conducted to identify SOST fragments with strong binding affinity for ROMO, revealing that SOST 114–143 and SOST 143–173 exhibit significantly higher affinity ( P <0.01). (B) A schematic diagram delineating the binding functional regions associated with the high-affinity fragments of SOST. (C) ELISA results indicate that SOST 131–163 displays the highest affinity for ROMO ( P <0.01), thereby identifying it as a potent functional epitope of SOST. (D-a) SOST 131–163 fragment (highlighted in yellow) is located within the loop3 domain of SOST protein. (D-b) Docking studies indicate that SOST 131–163 fragment interacts with ROMO light chain, yielding a binding free energy of -25.8 kcal/mol and an interface area of 712.9 Ų. (D-c) Additionally, SOST 131–163 fragment can bind to the ROMO heavy chain, resulting in a binding free energy of -33.19 kcal/mol and an interface area of 451.6 Ų. (E) CTL epitopes within SOST 131–163 sequence include two strong binder epitopes and four weak binder epitopes. (F) HTL epitopes in SOST 131–163 sequence comprise one strong binder epitope and four weak binder epitopes. Predictions of B cell epitopes for SOST 131–163 sequence are illustrated, including predicted linear B cell epitopes (G) and predicted discontinuous B cell epitopes (H) .

    Journal: Frontiers in Immunology

    Article Title: In silico design of novel precision vaccine targeting sclerostin epitopes for osteoporosis prevention and treatment

    doi: 10.3389/fimmu.2025.1644437

    Figure Lengend Snippet: Screening and analysis of high-affinity epitopes on SOST. (A) ELISA experiments were conducted to identify SOST fragments with strong binding affinity for ROMO, revealing that SOST 114–143 and SOST 143–173 exhibit significantly higher affinity ( P <0.01). (B) A schematic diagram delineating the binding functional regions associated with the high-affinity fragments of SOST. (C) ELISA results indicate that SOST 131–163 displays the highest affinity for ROMO ( P <0.01), thereby identifying it as a potent functional epitope of SOST. (D-a) SOST 131–163 fragment (highlighted in yellow) is located within the loop3 domain of SOST protein. (D-b) Docking studies indicate that SOST 131–163 fragment interacts with ROMO light chain, yielding a binding free energy of -25.8 kcal/mol and an interface area of 712.9 Ų. (D-c) Additionally, SOST 131–163 fragment can bind to the ROMO heavy chain, resulting in a binding free energy of -33.19 kcal/mol and an interface area of 451.6 Ų. (E) CTL epitopes within SOST 131–163 sequence include two strong binder epitopes and four weak binder epitopes. (F) HTL epitopes in SOST 131–163 sequence comprise one strong binder epitope and four weak binder epitopes. Predictions of B cell epitopes for SOST 131–163 sequence are illustrated, including predicted linear B cell epitopes (G) and predicted discontinuous B cell epitopes (H) .

    Article Snippet: In brief, 1 μg/mL of human SOST protein (MedChemExpress Inc.) was coated onto the wells of MaxiSorp microtiter plates (Thermo Fisher Scientific Inc.) and incubated overnight at 4°C.

    Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Functional Assay, Sequencing