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sphero™ polystyrene particles  (Spherotech inc)

 
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    Spherotech inc sphero™ polystyrene particles
    Sphero™ Polystyrene Particles, supplied by Spherotech inc, 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/sphero%E2%84%A2+polystyrene+particles/sphero+carboxyl+magnetic+blue+fluorescent+beads/us10890532-134-6-9
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    sphero™ polystyrene particles - by Bioz Stars, 2026-10
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    Article Title: Compositions and methods for performing assays
    Article Snippet: In at least on exemplary embodiment, SPHEROTM Polystyrene Particles, Spherotech, Lake Forest, Ill., may be used in multiplex assays.

    Article Title: Textured metallic back reflector
    Article Snippet: Resistive particles which are useful in embodiments described herein may be SPHERO™ polystyrene particles, such as PP-008-010 and PP025-10, commercially available from Spherotech, Inc. of Lake Forest, Ill.



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    (A) Ribbon diagram of KRIT1 FERM domain in complex with the HEG1 cytoplasmic tail (PDB ID: 3u7d). The HEG1 peptide is shown in yellow. The KRIT1 FERM domain consists of three subdomains: F1 (green and blue); F2 (red); and F3 (orange). The feature of the F1 domain that is not present in other FERM domain is shown in blue and that region is an important part of the HEG1 binding pocket. (B) Schematic representation of the HEG1 cytoplasmic tail (a.a. 1274-1381) peptide coupled to <t>Neutravidin</t> beads and of the EGFP-KRIT1 FERM domain. (C) Flow cytometry profile of <t>SPHERO</t> Neutravidin Polystyrene Particles coated with increasing amount of biotinylated HEG1 peptide and 150 nM EGFP-KRIT1 FERM domain. We noticed many beads doublets in the light scattering at 1,500 nM concentration of HEG1 peptide. (D) Titration curve for the interaction of EGFP-KRIT1 FERM domain with increasing amounts of HEG1 on the beads as shown in panel C. We used the 150 nM HEG1 peptide concentration for future experiments. (E) Titration curve for the interaction of 150 nM HEG1 on the beads with increasing amounts of EGFP-KRIT1 FERM domain (0-250 nM) wild-type (blue line) and KRIT1(L717,721A) mutant (red line). We used the 70 nM EGFP-KRIT1 concentration for future experiments. (F) Competition binding curve of 70 nM EGFP-KRIT1 FERM domain binding to 150 nM HEG1 on the beads with increasing amounts on non-biotinylated HEG1 7-mer peptide. We used the 2 μM HEG1 7-mer concentration for future experiments.
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    (A) Ribbon diagram of KRIT1 FERM domain in complex with the HEG1 cytoplasmic tail (PDB ID: 3u7d). The HEG1 peptide is shown in yellow. The KRIT1 FERM domain consists of three subdomains: F1 (green and blue); F2 (red); and F3 (orange). The feature of the F1 domain that is not present in other FERM domain is shown in blue and that region is an important part of the HEG1 binding pocket. (B) Schematic representation of the HEG1 cytoplasmic tail (a.a. 1274-1381) peptide coupled to <t>Neutravidin</t> beads and of the EGFP-KRIT1 FERM domain. (C) Flow cytometry profile of <t>SPHERO</t> Neutravidin Polystyrene Particles coated with increasing amount of biotinylated HEG1 peptide and 150 nM EGFP-KRIT1 FERM domain. We noticed many beads doublets in the light scattering at 1,500 nM concentration of HEG1 peptide. (D) Titration curve for the interaction of EGFP-KRIT1 FERM domain with increasing amounts of HEG1 on the beads as shown in panel C. We used the 150 nM HEG1 peptide concentration for future experiments. (E) Titration curve for the interaction of 150 nM HEG1 on the beads with increasing amounts of EGFP-KRIT1 FERM domain (0-250 nM) wild-type (blue line) and KRIT1(L717,721A) mutant (red line). We used the 70 nM EGFP-KRIT1 concentration for future experiments. (F) Competition binding curve of 70 nM EGFP-KRIT1 FERM domain binding to 150 nM HEG1 on the beads with increasing amounts on non-biotinylated HEG1 7-mer peptide. We used the 2 μM HEG1 7-mer concentration for future experiments.
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    (A) Ribbon diagram of KRIT1 FERM domain in complex with the HEG1 cytoplasmic tail (PDB ID: 3u7d). The HEG1 peptide is shown in yellow. The KRIT1 FERM domain consists of three subdomains: F1 (green and blue); F2 (red); and F3 (orange). The feature of the F1 domain that is not present in other FERM domain is shown in blue and that region is an important part of the HEG1 binding pocket. (B) Schematic representation of the HEG1 cytoplasmic tail (a.a. 1274-1381) peptide coupled to <t>Neutravidin</t> beads and of the EGFP-KRIT1 FERM domain. (C) Flow cytometry profile of <t>SPHERO</t> Neutravidin Polystyrene Particles coated with increasing amount of biotinylated HEG1 peptide and 150 nM EGFP-KRIT1 FERM domain. We noticed many beads doublets in the light scattering at 1,500 nM concentration of HEG1 peptide. (D) Titration curve for the interaction of EGFP-KRIT1 FERM domain with increasing amounts of HEG1 on the beads as shown in panel C. We used the 150 nM HEG1 peptide concentration for future experiments. (E) Titration curve for the interaction of 150 nM HEG1 on the beads with increasing amounts of EGFP-KRIT1 FERM domain (0-250 nM) wild-type (blue line) and KRIT1(L717,721A) mutant (red line). We used the 70 nM EGFP-KRIT1 concentration for future experiments. (F) Competition binding curve of 70 nM EGFP-KRIT1 FERM domain binding to 150 nM HEG1 on the beads with increasing amounts on non-biotinylated HEG1 7-mer peptide. We used the 2 μM HEG1 7-mer concentration for future experiments.
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    (A) Ribbon diagram of KRIT1 FERM domain in complex with the HEG1 cytoplasmic tail (PDB ID: 3u7d). The HEG1 peptide is shown in yellow. The KRIT1 FERM domain consists of three subdomains: F1 (green and blue); F2 (red); and F3 (orange). The feature of the F1 domain that is not present in other FERM domain is shown in blue and that region is an important part of the HEG1 binding pocket. (B) Schematic representation of the HEG1 cytoplasmic tail (a.a. 1274-1381) peptide coupled to <t>Neutravidin</t> beads and of the EGFP-KRIT1 FERM domain. (C) Flow cytometry profile of <t>SPHERO</t> Neutravidin Polystyrene Particles coated with increasing amount of biotinylated HEG1 peptide and 150 nM EGFP-KRIT1 FERM domain. We noticed many beads doublets in the light scattering at 1,500 nM concentration of HEG1 peptide. (D) Titration curve for the interaction of EGFP-KRIT1 FERM domain with increasing amounts of HEG1 on the beads as shown in panel C. We used the 150 nM HEG1 peptide concentration for future experiments. (E) Titration curve for the interaction of 150 nM HEG1 on the beads with increasing amounts of EGFP-KRIT1 FERM domain (0-250 nM) wild-type (blue line) and KRIT1(L717,721A) mutant (red line). We used the 70 nM EGFP-KRIT1 concentration for future experiments. (F) Competition binding curve of 70 nM EGFP-KRIT1 FERM domain binding to 150 nM HEG1 on the beads with increasing amounts on non-biotinylated HEG1 7-mer peptide. We used the 2 μM HEG1 7-mer concentration for future experiments.
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    (A) Ribbon diagram of KRIT1 FERM domain in complex with the HEG1 cytoplasmic tail (PDB ID: 3u7d). The HEG1 peptide is shown in yellow. The KRIT1 FERM domain consists of three subdomains: F1 (green and blue); F2 (red); and F3 (orange). The feature of the F1 domain that is not present in other FERM domain is shown in blue and that region is an important part of the HEG1 binding pocket. (B) Schematic representation of the HEG1 cytoplasmic tail (a.a. 1274-1381) peptide coupled to <t>Neutravidin</t> beads and of the EGFP-KRIT1 FERM domain. (C) Flow cytometry profile of <t>SPHERO</t> Neutravidin Polystyrene Particles coated with increasing amount of biotinylated HEG1 peptide and 150 nM EGFP-KRIT1 FERM domain. We noticed many beads doublets in the light scattering at 1,500 nM concentration of HEG1 peptide. (D) Titration curve for the interaction of EGFP-KRIT1 FERM domain with increasing amounts of HEG1 on the beads as shown in panel C. We used the 150 nM HEG1 peptide concentration for future experiments. (E) Titration curve for the interaction of 150 nM HEG1 on the beads with increasing amounts of EGFP-KRIT1 FERM domain (0-250 nM) wild-type (blue line) and KRIT1(L717,721A) mutant (red line). We used the 70 nM EGFP-KRIT1 concentration for future experiments. (F) Competition binding curve of 70 nM EGFP-KRIT1 FERM domain binding to 150 nM HEG1 on the beads with increasing amounts on non-biotinylated HEG1 7-mer peptide. We used the 2 μM HEG1 7-mer concentration for future experiments.
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    (A) Ribbon diagram of KRIT1 FERM domain in complex with the HEG1 cytoplasmic tail (PDB ID: 3u7d). The HEG1 peptide is shown in yellow. The KRIT1 FERM domain consists of three subdomains: F1 (green and blue); F2 (red); and F3 (orange). The feature of the F1 domain that is not present in other FERM domain is shown in blue and that region is an important part of the HEG1 binding pocket. (B) Schematic representation of the HEG1 cytoplasmic tail (a.a. 1274-1381) peptide coupled to <t>Neutravidin</t> beads and of the EGFP-KRIT1 FERM domain. (C) Flow cytometry profile of <t>SPHERO</t> Neutravidin Polystyrene Particles coated with increasing amount of biotinylated HEG1 peptide and 150 nM EGFP-KRIT1 FERM domain. We noticed many beads doublets in the light scattering at 1,500 nM concentration of HEG1 peptide. (D) Titration curve for the interaction of EGFP-KRIT1 FERM domain with increasing amounts of HEG1 on the beads as shown in panel C. We used the 150 nM HEG1 peptide concentration for future experiments. (E) Titration curve for the interaction of 150 nM HEG1 on the beads with increasing amounts of EGFP-KRIT1 FERM domain (0-250 nM) wild-type (blue line) and KRIT1(L717,721A) mutant (red line). We used the 70 nM EGFP-KRIT1 concentration for future experiments. (F) Competition binding curve of 70 nM EGFP-KRIT1 FERM domain binding to 150 nM HEG1 on the beads with increasing amounts on non-biotinylated HEG1 7-mer peptide. We used the 2 μM HEG1 7-mer concentration for future experiments.
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    Image Search Results


    (A) Ribbon diagram of KRIT1 FERM domain in complex with the HEG1 cytoplasmic tail (PDB ID: 3u7d). The HEG1 peptide is shown in yellow. The KRIT1 FERM domain consists of three subdomains: F1 (green and blue); F2 (red); and F3 (orange). The feature of the F1 domain that is not present in other FERM domain is shown in blue and that region is an important part of the HEG1 binding pocket. (B) Schematic representation of the HEG1 cytoplasmic tail (a.a. 1274-1381) peptide coupled to Neutravidin beads and of the EGFP-KRIT1 FERM domain. (C) Flow cytometry profile of SPHERO Neutravidin Polystyrene Particles coated with increasing amount of biotinylated HEG1 peptide and 150 nM EGFP-KRIT1 FERM domain. We noticed many beads doublets in the light scattering at 1,500 nM concentration of HEG1 peptide. (D) Titration curve for the interaction of EGFP-KRIT1 FERM domain with increasing amounts of HEG1 on the beads as shown in panel C. We used the 150 nM HEG1 peptide concentration for future experiments. (E) Titration curve for the interaction of 150 nM HEG1 on the beads with increasing amounts of EGFP-KRIT1 FERM domain (0-250 nM) wild-type (blue line) and KRIT1(L717,721A) mutant (red line). We used the 70 nM EGFP-KRIT1 concentration for future experiments. (F) Competition binding curve of 70 nM EGFP-KRIT1 FERM domain binding to 150 nM HEG1 on the beads with increasing amounts on non-biotinylated HEG1 7-mer peptide. We used the 2 μM HEG1 7-mer concentration for future experiments.

    Journal: bioRxiv

    Article Title: Pharmacological inhibition of the heart of glass (HEG1)-Krev interaction trapped protein 1 (KRIT1) protein complex increases Krüppel-like Factors 4 and 2 (KLF4/2) expression in endothelial cells

    doi: 10.1101/744821

    Figure Lengend Snippet: (A) Ribbon diagram of KRIT1 FERM domain in complex with the HEG1 cytoplasmic tail (PDB ID: 3u7d). The HEG1 peptide is shown in yellow. The KRIT1 FERM domain consists of three subdomains: F1 (green and blue); F2 (red); and F3 (orange). The feature of the F1 domain that is not present in other FERM domain is shown in blue and that region is an important part of the HEG1 binding pocket. (B) Schematic representation of the HEG1 cytoplasmic tail (a.a. 1274-1381) peptide coupled to Neutravidin beads and of the EGFP-KRIT1 FERM domain. (C) Flow cytometry profile of SPHERO Neutravidin Polystyrene Particles coated with increasing amount of biotinylated HEG1 peptide and 150 nM EGFP-KRIT1 FERM domain. We noticed many beads doublets in the light scattering at 1,500 nM concentration of HEG1 peptide. (D) Titration curve for the interaction of EGFP-KRIT1 FERM domain with increasing amounts of HEG1 on the beads as shown in panel C. We used the 150 nM HEG1 peptide concentration for future experiments. (E) Titration curve for the interaction of 150 nM HEG1 on the beads with increasing amounts of EGFP-KRIT1 FERM domain (0-250 nM) wild-type (blue line) and KRIT1(L717,721A) mutant (red line). We used the 70 nM EGFP-KRIT1 concentration for future experiments. (F) Competition binding curve of 70 nM EGFP-KRIT1 FERM domain binding to 150 nM HEG1 on the beads with increasing amounts on non-biotinylated HEG1 7-mer peptide. We used the 2 μM HEG1 7-mer concentration for future experiments.

    Article Snippet: SPHERO Neutravidin Polystyrene Particles, 6-8 μM (Spherotech) were washed twice with wash buffer (20 mM Tris, 150 mM NaCl, pH 7.4 containing 0.01% NP-40, and 1mM EDTA).

    Techniques: Binding Assay, Flow Cytometry, Concentration Assay, Titration, Mutagenesis