eeg analysis software chart 8.1.5 Search Results


96
JASCO Inc j 1500 instrument
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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emka TECHNOLOGIES S A S ecg-auto version 1.5.8.15
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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99
STATA Corporation seerstat version 8 1 5
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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JASCO Inc j700 software
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
J700 Software, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
ASYST Technologies Inc nanoscope analysis scan asyst software
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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90
ZYGO Corp metropro version 8.1.5
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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86
Biomatters Ltd geneious 8 1 5
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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90
BioReliance x-mulv pnfs th-1
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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90
Scanditronix gmbh pc-2048b 15 slice pet acquisition system
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
Pc 2048b 15 Slice Pet Acquisition System, supplied by Scanditronix gmbh, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
OriginLab corp originpro 8.1.5
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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90
ZEMAX Development Corporation elcomat-3000/8,15
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
Elcomat 3000/8,15, supplied by ZEMAX Development Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
2mag AG optical extinction
Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO <t>J-1500</t> circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.
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Image Search Results


Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO J-1500 circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.

Journal: Frontiers in Cell and Developmental Biology

Article Title: The Impact of Rare Human Variants on Barrier-To-Auto-Integration Factor 1 (Banf1) Structure and Function

doi: 10.3389/fcell.2021.775441

Figure Lengend Snippet: Banf1 variants do not significantly alter Banf1 secondary structure. (A) Banf1 His-tagged WT and variant proteins were expressed and purified from E.coli cells. Purified proteins were run on an SDS PAGE gel and stained with Coomassie. (B) Representative molecular ellipticity trace over a wavelength of 185–260 nm (n = 3). The molecular ellipticity values were calculated based the molar concentration of each protein sample and the CD values, which were obtained using JASCO J-1500 circular dichroism spectrophotometer. (C) Representative curve fitting of thermal stability analysis of point CD measurements at 222 nm over a temperature gradient from 10 to 90°C, taken in three technical repeats every 0.1°C. (D) Thermal disassociation temperature of Banf1 wild-type, H7Y, D9H, D9N, S22R, N70T, R75W, and G79R variants.

Article Snippet: All CD spectra data was analysed using software provided with the JASCO J-1500 instrument.

Techniques: Variant Assay, Purification, SDS Page, Staining, Concentration Assay, Spectrophotometry