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OriginLab originpro software
Originpro Software, supplied by OriginLab, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/originpro software/product/OriginLab
Average 99 stars, based on 1 article reviews
Price from $9.99 to $1999.99
originpro software - by Bioz Stars, 2022-09
99/100 stars

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  • 98
    OriginLab pro 8 software
    Preparation of the biosensor for measurements. (a) Electrical contacts to the prepared devices are made with copper tape, platinum foil (as the counter electrode) and alligator pins. (b) Measurements were performed using a PalmSens3 analyzer controlled by PS-Trace 4.8. Data was processed with GNU Octave, Igor Pro, and OriginLab Pro 8.
    Pro 8 Software, supplied by OriginLab, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pro 8 software/product/OriginLab
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pro 8 software - by Bioz Stars, 2022-09
    98/100 stars
      Buy from Supplier

    99
    OriginLab originpro 8 software
    Unfolding and refolding kinetics of MsEis protein. Intrinsic tryptophan fluorescence spectra of either unfolded or refolded MsEis protein in the presence or absence of GdmCl and urea at different time intervals. 0 h  (Panel A) , 2 h  (Panel B) , 4 h  (panel C) , 6 h  (Panel D) , 8 h  (Panel E) , 10 h  (Panel F)  and 12 h  (Panel G) . The values corresponding to native MsEis without treatment were considered as 100% in each case of unfolding or refolding. The values obtained from emission maxima were fitted using OriginPro 8.0 software.
    Originpro 8 Software, supplied by OriginLab, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/originpro 8 software/product/OriginLab
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    originpro 8 software - by Bioz Stars, 2022-09
    99/100 stars
      Buy from Supplier

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    Preparation of the biosensor for measurements. (a) Electrical contacts to the prepared devices are made with copper tape, platinum foil (as the counter electrode) and alligator pins. (b) Measurements were performed using a PalmSens3 analyzer controlled by PS-Trace 4.8. Data was processed with GNU Octave, Igor Pro, and OriginLab Pro 8.

    Journal: ACS applied materials & interfaces

    Article Title: Electrochemical quantification of glycated and non-glycated human serum albumin in synthetic urine

    doi: 10.1021/acsami.8b16071

    Figure Lengend Snippet: Preparation of the biosensor for measurements. (a) Electrical contacts to the prepared devices are made with copper tape, platinum foil (as the counter electrode) and alligator pins. (b) Measurements were performed using a PalmSens3 analyzer controlled by PS-Trace 4.8. Data was processed with GNU Octave, Igor Pro, and OriginLab Pro 8.

    Article Snippet: All electrochemical data was processed on GNU Octave, Igor Pro and OriginLab Pro 8 software.

    Techniques:

    Unfolding and refolding kinetics of MsEis protein. Intrinsic tryptophan fluorescence spectra of either unfolded or refolded MsEis protein in the presence or absence of GdmCl and urea at different time intervals. 0 h  (Panel A) , 2 h  (Panel B) , 4 h  (panel C) , 6 h  (Panel D) , 8 h  (Panel E) , 10 h  (Panel F)  and 12 h  (Panel G) . The values corresponding to native MsEis without treatment were considered as 100% in each case of unfolding or refolding. The values obtained from emission maxima were fitted using OriginPro 8.0 software.

    Journal: PLoS ONE

    Article Title: Differential thermal stability, conformational stability and unfolding behavior of Eis proteins from Mycobacterium smegmatis and Mycobacterium tuberculosis

    doi: 10.1371/journal.pone.0213933

    Figure Lengend Snippet: Unfolding and refolding kinetics of MsEis protein. Intrinsic tryptophan fluorescence spectra of either unfolded or refolded MsEis protein in the presence or absence of GdmCl and urea at different time intervals. 0 h (Panel A) , 2 h (Panel B) , 4 h (panel C) , 6 h (Panel D) , 8 h (Panel E) , 10 h (Panel F) and 12 h (Panel G) . The values corresponding to native MsEis without treatment were considered as 100% in each case of unfolding or refolding. The values obtained from emission maxima were fitted using OriginPro 8.0 software.

    Article Snippet: The obtained data points were fitted to three-state model (biDose-response curve of nonlinear regression analysis) using OriginPro 8 software (Origin Lab, Northampton, USA).

    Techniques: Fluorescence, Software

    Time kinetics, temperature stability and steady-state kinetic parameters of KAN acetylation by MsEis and RvEis. Time course of changes in the absorbance at 412 nm of NTB -  ions formed as a result of acetyltransferase activity of MsEis and RvEis proteins  (Panel A) . The effect of temperature on the catalytic activity of MsEis and RvEis was determined after incubating the Eis proteins at different temperatures ranging from 20°C to 80°C  (Panel B) . Kinetic parameters were calculated for the acetylation of KAN by MsEis and RvEis at fixed concentration of acetyl CoA and increasing concentration of KAN antibiotic  (Panel C) . The experimental values were fitted to Michaelis-Menten equation using OriginPro 8.0 software (Origin Labs, Northampton, USA).

    Journal: PLoS ONE

    Article Title: Differential thermal stability, conformational stability and unfolding behavior of Eis proteins from Mycobacterium smegmatis and Mycobacterium tuberculosis

    doi: 10.1371/journal.pone.0213933

    Figure Lengend Snippet: Time kinetics, temperature stability and steady-state kinetic parameters of KAN acetylation by MsEis and RvEis. Time course of changes in the absorbance at 412 nm of NTB - ions formed as a result of acetyltransferase activity of MsEis and RvEis proteins (Panel A) . The effect of temperature on the catalytic activity of MsEis and RvEis was determined after incubating the Eis proteins at different temperatures ranging from 20°C to 80°C (Panel B) . Kinetic parameters were calculated for the acetylation of KAN by MsEis and RvEis at fixed concentration of acetyl CoA and increasing concentration of KAN antibiotic (Panel C) . The experimental values were fitted to Michaelis-Menten equation using OriginPro 8.0 software (Origin Labs, Northampton, USA).

    Article Snippet: The obtained data points were fitted to three-state model (biDose-response curve of nonlinear regression analysis) using OriginPro 8 software (Origin Lab, Northampton, USA).

    Techniques: Activity Assay, Impedance Spectroscopy, Concentration Assay, Software

    Comparison of conformational stability of MsEis and RvEis proteins in the presence of different denaturants. Intrinsic tryptophan fluorescence spectra of MsEis and RvEis proteins in the presence of increasing concentration of GdmCl  (Panel A),  urea  (Panel C)  and at increasing temperature from 25°C to 100°C  (Panel E) . Unfolding of MsEis and RvEis proteins measured in terms of changes in emission wavelength maxima in the presence of GdmCl  (Panel B),  urea  (panel D)  and temperature  (Panel F) . The values corresponding to native Eis without treatment were considered as 100%. Fitting of the values obtained from emission maxima were done by using equations with OriginPro 8.0 software.

    Journal: PLoS ONE

    Article Title: Differential thermal stability, conformational stability and unfolding behavior of Eis proteins from Mycobacterium smegmatis and Mycobacterium tuberculosis

    doi: 10.1371/journal.pone.0213933

    Figure Lengend Snippet: Comparison of conformational stability of MsEis and RvEis proteins in the presence of different denaturants. Intrinsic tryptophan fluorescence spectra of MsEis and RvEis proteins in the presence of increasing concentration of GdmCl (Panel A), urea (Panel C) and at increasing temperature from 25°C to 100°C (Panel E) . Unfolding of MsEis and RvEis proteins measured in terms of changes in emission wavelength maxima in the presence of GdmCl (Panel B), urea (panel D) and temperature (Panel F) . The values corresponding to native Eis without treatment were considered as 100%. Fitting of the values obtained from emission maxima were done by using equations with OriginPro 8.0 software.

    Article Snippet: The obtained data points were fitted to three-state model (biDose-response curve of nonlinear regression analysis) using OriginPro 8 software (Origin Lab, Northampton, USA).

    Techniques: Fluorescence, Concentration Assay, Impedance Spectroscopy, Software

    Evaluation of three internal reference candidates in monoculture and syntrophic dual-culture. C T  is the qPCR quantification cycle, the fractional cycle number where fluorescence increases above the threshold. 13 cells from monoculture and 13 cells from syntrophic dual-culture were used to evaluate the consistency of the internal reference genes. The standard deviations (SD) across single cells were calculated using the OriginPro 8.0 software. Mean Ct values and SD values calculated using 13 single cells from each of the two conditions ( i.e. , mono- or dual-cultures) were shown above the plots.

    Journal: Scientific Reports

    Article Title: Single-cell analysis reveals gene-expression heterogeneity in syntrophic dual-culture of Desulfovibrio vulgaris with Methanosarcina barkeri

    doi: 10.1038/srep07478

    Figure Lengend Snippet: Evaluation of three internal reference candidates in monoculture and syntrophic dual-culture. C T is the qPCR quantification cycle, the fractional cycle number where fluorescence increases above the threshold. 13 cells from monoculture and 13 cells from syntrophic dual-culture were used to evaluate the consistency of the internal reference genes. The standard deviations (SD) across single cells were calculated using the OriginPro 8.0 software. Mean Ct values and SD values calculated using 13 single cells from each of the two conditions ( i.e. , mono- or dual-cultures) were shown above the plots.

    Article Snippet: Kolmogorov-Smirnov, Kruskal-Wallis and Mann-Whitney analysis of variance (ANOVA) tests were also used to analyze the relationship between four different groups of RT-qPCR measurements using the OriginPro 8.0 software (OriginLab Corporation, Northampton, MA).

    Techniques: Real-time Polymerase Chain Reaction, Fluorescence, Software

    Silver content variations in different culture media, at 0 and 24 h of incubation. There are significant differences in the silver content in the different culture media over time. One-way ANOVA was performed on the replicates of each treatment followed by Tukey’s multiple comparison post-test, using the software OriginPro 8 (OriginLab), * = p

    Journal: ACS Omega

    Article Title: Beyond the Nanomaterials Approach: Influence of Culture Conditions on the Stability and Antimicrobial Activity of Silver Nanoparticles

    doi: 10.1021/acsomega.0c02007

    Figure Lengend Snippet: Silver content variations in different culture media, at 0 and 24 h of incubation. There are significant differences in the silver content in the different culture media over time. One-way ANOVA was performed on the replicates of each treatment followed by Tukey’s multiple comparison post-test, using the software OriginPro 8 (OriginLab), * = p

    Article Snippet: The statistical analysis was performed via one-way ANOVA with Tukey’s multiple comparison post-test, with the OriginPro 8 software (OriginLab).

    Techniques: Incubation, Software

    Effect of culture media on bacterial growth. E. coli was cultured in different media, with no AgNPs. Growth in MH was set as 100%. One-way ANOVA was performed on the replicates of each treatment followed by Tukey’s multiple comparison post-test, using the software OriginPro 8 (OriginLab), * = p

    Journal: ACS Omega

    Article Title: Beyond the Nanomaterials Approach: Influence of Culture Conditions on the Stability and Antimicrobial Activity of Silver Nanoparticles

    doi: 10.1021/acsomega.0c02007

    Figure Lengend Snippet: Effect of culture media on bacterial growth. E. coli was cultured in different media, with no AgNPs. Growth in MH was set as 100%. One-way ANOVA was performed on the replicates of each treatment followed by Tukey’s multiple comparison post-test, using the software OriginPro 8 (OriginLab), * = p

    Article Snippet: The statistical analysis was performed via one-way ANOVA with Tukey’s multiple comparison post-test, with the OriginPro 8 software (OriginLab).

    Techniques: Cell Culture, Software