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fastfit software  (Thermo Fisher)


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    Thermo Fisher fastfit software
    Fastfit Software, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fastfit/pmc05408269-329-35-37
    Average 86 stars, based on 1 article reviews
    fastfit software - by Bioz Stars, 2026-09
    86/100 stars

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    Related Articles

    Binding Assay:

    Article Title: Interactions of Multiple Heparin Binding Growth Factors with Neuropilin-1 and Potentiation of the Activity of Fibroblast Growth Factor-2
    Article Snippet: .. Binding parameters were calculated from the association and dissociation phases of the binding reactions using the non-linear curve fitting FASTfit (Thermo Electron). ..

    Article Title: Synthetic Human TLR9-LRR11 Peptide Attenuates TLR9 Signaling by Binding to and thus Decreasing Internalization of CpG Oligodeoxynucleotides
    Article Snippet: .. Binding curves were analyzed and visualized using FASTplot (Thermo), and the dissociation equilibrium constant (K D ) of SP with ODN2006 was calculated using FASTfit (Thermo). .. The Biacore3000 system (GE Healthcare, Uppsala, Sweden) was applied to reproduce the results of IAsys biosensor essentially as described previously [ ].

    Software:

    Article Title: The newly identified CpG-N ODN208 protects mice from challenge with CpG-S ODN by decreasing TNF-alpha release.
    Article Snippet: Administration of an excess of oligodeoxynucleotides containing immunostimulatory CpG motifs (CpG-S ODNs) may induce systemic inflammatory response syndrome (SIRS) and sepsis.. Therefore, it is important to develop neutralizing CpG ODNs (CpGN ODNs), which can be used to reduce the release of cytokines induced by the presence of CpG-S ODNs.. In the present study, CpG-N ODN208 (5′-TGCCGCGGCAGA-3′), a neutralizing twelve-oligodeoxynucleotide molecule recently identified in our laboratory, inhibited TNF-α release from human peripheral blood mononuclear cells (hPBMCs) and murine RAW264.7 cells induced by CpG-S ODN exposure in a doseand time-dependent manner.



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    Synthetic peptide (SP) specifically binds ODN2006. ( A ) Binding curves generated by the IAsys biosensor. Biotinylated ODN2006 was immobilized on the surface of a streptavidin-coated cuvette. A series of concentration of SP (3.1, 6.3, 12.5, 25 or 50 μM) or unrelated peptide (URP) (50 μM) were added separately into the cuvette to generate the binding curves. Data were analyzed using FASTplot, and the dissociation equilibrium constant (K D ) of SP was calculated using <t>FASTfit;</t> ( B ) Binding curves generated by the Biacore biosensor. Biotinylated ODN2006 was immobilized on a streptavidin-coated chip, and then a series of concentrations of SP (0.63, 1.25, 2.5, 5 or 10 μM) or URP (10 μM) were loaded separately to generate the binding curves. Data analysis and K D calculation were performed using the BIAevaluation software.
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    Image Search Results


    Visualization of the rich angle-correlated X-ray spectrum of a simulated LCS output with a Compton edge (ECE) of 60 keV at observation angles (θx, θy) up to 5 mrad from the center of the beam profile. On the X-ray flux density plot (left), four regions of interest are highlighted with dashed lines. (a) The entire field of view, (b) a centered annulus, (c) the center, and (d) an off-center region of the LCS X-ray spectrum are highlighted, and the relative total flux and energy spectrum through these regions is illustrated (right). The LCS interaction parameters used to generate these plots are described in more detail in Section 2.1 and are assumed for all LCS X-ray distributions simulated in this paper.

    Journal: Applied optics

    Article Title: Computational method for the optimization of quasimonoenergetic Laser Compton X-ray sources for imaging applications

    doi: 10.1364/AO.444307

    Figure Lengend Snippet: Visualization of the rich angle-correlated X-ray spectrum of a simulated LCS output with a Compton edge (ECE) of 60 keV at observation angles (θx, θy) up to 5 mrad from the center of the beam profile. On the X-ray flux density plot (left), four regions of interest are highlighted with dashed lines. (a) The entire field of view, (b) a centered annulus, (c) the center, and (d) an off-center region of the LCS X-ray spectrum are highlighted, and the relative total flux and energy spectrum through these regions is illustrated (right). The LCS interaction parameters used to generate these plots are described in more detail in Section 2.1 and are assumed for all LCS X-ray distributions simulated in this paper.

    Article Snippet: All Compton FastFit code was written and tested in MATLAB R2021a and can be accessed with explicit instructions on how to generate the data that will be presented and discussed in this paper [ 30 , 31 ].

    Techniques:

    Visualization of the change in shape of local X-ray distributions as a function of observation angle (θx) from an LCS interaction with a Compton edge (ECE) of 60 keV.

    Journal: Applied optics

    Article Title: Computational method for the optimization of quasimonoenergetic Laser Compton X-ray sources for imaging applications

    doi: 10.1364/AO.444307

    Figure Lengend Snippet: Visualization of the change in shape of local X-ray distributions as a function of observation angle (θx) from an LCS interaction with a Compton edge (ECE) of 60 keV.

    Article Snippet: All Compton FastFit code was written and tested in MATLAB R2021a and can be accessed with explicit instructions on how to generate the data that will be presented and discussed in this paper [ 30 , 31 ].

    Techniques:

    Comparison of FastFit interpolation and LCS code at two observation angles whose values are in mrad.

    Journal: Applied optics

    Article Title: Computational method for the optimization of quasimonoenergetic Laser Compton X-ray sources for imaging applications

    doi: 10.1364/AO.444307

    Figure Lengend Snippet: Comparison of FastFit interpolation and LCS code at two observation angles whose values are in mrad.

    Article Snippet: All Compton FastFit code was written and tested in MATLAB R2021a and can be accessed with explicit instructions on how to generate the data that will be presented and discussed in this paper [ 30 , 31 ].

    Techniques: Comparison

    Synthetic peptide (SP) specifically binds ODN2006. ( A ) Binding curves generated by the IAsys biosensor. Biotinylated ODN2006 was immobilized on the surface of a streptavidin-coated cuvette. A series of concentration of SP (3.1, 6.3, 12.5, 25 or 50 μM) or unrelated peptide (URP) (50 μM) were added separately into the cuvette to generate the binding curves. Data were analyzed using FASTplot, and the dissociation equilibrium constant (K D ) of SP was calculated using FASTfit; ( B ) Binding curves generated by the Biacore biosensor. Biotinylated ODN2006 was immobilized on a streptavidin-coated chip, and then a series of concentrations of SP (0.63, 1.25, 2.5, 5 or 10 μM) or URP (10 μM) were loaded separately to generate the binding curves. Data analysis and K D calculation were performed using the BIAevaluation software.

    Journal: International Journal of Molecular Sciences

    Article Title: Synthetic Human TLR9-LRR11 Peptide Attenuates TLR9 Signaling by Binding to and thus Decreasing Internalization of CpG Oligodeoxynucleotides

    doi: 10.3390/ijms17020242

    Figure Lengend Snippet: Synthetic peptide (SP) specifically binds ODN2006. ( A ) Binding curves generated by the IAsys biosensor. Biotinylated ODN2006 was immobilized on the surface of a streptavidin-coated cuvette. A series of concentration of SP (3.1, 6.3, 12.5, 25 or 50 μM) or unrelated peptide (URP) (50 μM) were added separately into the cuvette to generate the binding curves. Data were analyzed using FASTplot, and the dissociation equilibrium constant (K D ) of SP was calculated using FASTfit; ( B ) Binding curves generated by the Biacore biosensor. Biotinylated ODN2006 was immobilized on a streptavidin-coated chip, and then a series of concentrations of SP (0.63, 1.25, 2.5, 5 or 10 μM) or URP (10 μM) were loaded separately to generate the binding curves. Data analysis and K D calculation were performed using the BIAevaluation software.

    Article Snippet: Binding curves were analyzed and visualized using FASTplot (Thermo), and the dissociation equilibrium constant (K D ) of SP with ODN2006 was calculated using FASTfit (Thermo).

    Techniques: Binding Assay, Generated, Concentration Assay, Software