envelope e protein Search Results


mouse anti-pan flavivirus envelope e protein monoclonal antibody (4g2)  (RD Biotech)
90
RD Biotech mouse anti-pan flavivirus envelope e protein monoclonal antibody (4g2)
Mouse Anti Pan Flavivirus Envelope E Protein Monoclonal Antibody (4g2), supplied by RD Biotech, 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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anti-flavivirus mouse monoclonal antibody d1-4g2-4-15 (4g2  (Absolute Biotech)
90
Absolute Biotech anti-flavivirus mouse monoclonal antibody d1-4g2-4-15 (4g2
Anti Flavivirus Mouse Monoclonal Antibody D1 4g2 4 15 (4g2, supplied by Absolute Biotech, 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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zikv envelope (e) zikv nonstructural (ns)1 ns1s of den 1—den 4 recombinant protein antigens  (Meridian Bioscience)
90
Meridian Bioscience zikv envelope (e) zikv nonstructural (ns)1 ns1s of den 1—den 4 recombinant protein antigens
Zikv Envelope (E) Zikv Nonstructural (Ns)1 Ns1s Of Den 1—Den 4 Recombinant Protein Antigens, supplied by Meridian Bioscience, 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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coronavirus envelope (e) proteins  (Biodesign International Inc)
90
Biodesign International Inc coronavirus envelope (e) proteins
Coronavirus Envelope (E) Proteins, supplied by Biodesign International 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/result/coronavirus envelope (e) proteins/product/Biodesign International Inc
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recombinant envelope (e) protein mbs143155  (MyBiosource Biotechnology)
90
MyBiosource Biotechnology recombinant envelope (e) protein mbs143155
( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized <t>recombinant</t> JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.
Recombinant Envelope (E) Protein Mbs143155, supplied by MyBiosource Biotechnology, 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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recombinant envelope (e) protein mbs143155 - by Bioz Stars, 2026-03
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envelope e-protein (mbs8309649)  (MyBiosource Biotechnology)
90
MyBiosource Biotechnology envelope e-protein (mbs8309649)
( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized <t>recombinant</t> JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.
Envelope E Protein (Mbs8309649), supplied by MyBiosource Biotechnology, 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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antibodies against yfv envelope (e) protein  (GeneTex)
90
GeneTex antibodies against yfv envelope (e) protein
( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized <t>recombinant</t> JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.
Antibodies Against Yfv Envelope (E) Protein, supplied by GeneTex, 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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anti-fitc-labeled 4g2 ab (pan-flaviviral envelope [e] protein)  (Becton Dickinson)
90
Becton Dickinson anti-fitc-labeled 4g2 ab (pan-flaviviral envelope [e] protein)
( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized <t>recombinant</t> JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.
Anti Fitc Labeled 4g2 Ab (Pan Flaviviral Envelope [E] Protein), supplied by Becton Dickinson, 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/result/anti-fitc-labeled 4g2 ab (pan-flaviviral envelope [e] protein)/product/Becton Dickinson
Average 90 stars, based on 1 article reviews
anti-fitc-labeled 4g2 ab (pan-flaviviral envelope [e] protein) - by Bioz Stars, 2026-03
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dynamics late endosomal membrane flavivirus dengue envelope e protein membrane fusion  (Molecular Dynamics Inc)
90
Molecular Dynamics Inc dynamics late endosomal membrane flavivirus dengue envelope e protein membrane fusion
( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized <t>recombinant</t> JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.
Dynamics Late Endosomal Membrane Flavivirus Dengue Envelope E Protein Membrane Fusion, supplied by Molecular Dynamics 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/result/dynamics late endosomal membrane flavivirus dengue envelope e protein membrane fusion/product/Molecular Dynamics Inc
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dynamics late endosomal membrane flavivirus dengue envelope e protein membrane fusion - by Bioz Stars, 2026-03
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sars-related coronavirus 2 envelope (e) protein nr-52405  (BEI Resources)
90
BEI Resources sars-related coronavirus 2 envelope (e) protein nr-52405
( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized <t>recombinant</t> JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.
Sars Related Coronavirus 2 Envelope (E) Protein Nr 52405, supplied by BEI Resources, 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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real-time rt-pcr assays targeting the rna-dependent rna polymerase (rdrp) gene and envelope (e) protein gene  (Kogene Biotech)
90
Kogene Biotech real-time rt-pcr assays targeting the rna-dependent rna polymerase (rdrp) gene and envelope (e) protein gene
( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized <t>recombinant</t> JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.
Real Time Rt Pcr Assays Targeting The Rna Dependent Rna Polymerase (Rdrp) Gene And Envelope (E) Protein Gene, supplied by Kogene Biotech, 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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real-time rt-pcr assays targeting the rna-dependent rna polymerase (rdrp) gene and envelope (e) protein gene - by Bioz Stars, 2026-03
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envelope (e) protein  (ABclonal Biotechnology)
90
ABclonal Biotechnology envelope (e) protein
( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized <t>recombinant</t> JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.
Envelope (E) Protein, supplied by ABclonal Biotechnology, 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/result/envelope (e) protein/product/ABclonal Biotechnology
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envelope (e) protein - by Bioz Stars, 2026-03
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Image Search Results


( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized recombinant JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.

Journal: Scientific Reports

Article Title: Neutralization of Japanese Encephalitis Virus by heme-induced broadly reactive human monoclonal antibody

doi: 10.1038/srep16248

Figure Lengend Snippet: ( A ) Real-time interaction profiles of binding of native or heme-exposed human monoclonal IgG1, mAb21 to immobilized recombinant JEV E and EDIII proteins. The real-time interaction profiles obtained after injection of native mAb21, diluted to 500 nM are presented in the left panels. The binding profiles of heme-exposed mAb21 at 500, 250, 125, 62.5, 31.25, 15.63, 7.81, and 3.90 nM are presented on the right panels. The binding analyses were performed at 25 °C. The graphs show experimentally determined binding curves (black lines) and curves generated by globally fitting the data by BIA evaluation software (red line). The estimated kinetic parameters are presented on . ( B ) Arrhenius plots showing the natural logarithm values of association and dissociation rate constants of the heme-sensitive mAb21 obtained after interaction with JEV E (open circles) and JEV EDIII (filled circles) as a function of reciprocal values of temperature (in Kelvins). To generate these plots the kinetic rate constants were determined by global analysis of sensorgrams generated after evaluation of binding kinetics of the heme-exposed mAb21 with immobilized JEV proteins at varying temperatures (10, 15, 20, 25, 30, and 35 °C). Linear regression analyses were applied to obtain the slopes of the temperature dependency. ( C ) Association, dissociation and equilibrium thermodynamic parameters of binding of heme-exposed mAb21 to JEV E and EDIII. Changes in the enthalpy, entropy and free energy during different phases of the interaction of heme-exposed mAb21 with JEV E (white bars) and EDIII (black bars) are depicted. The changes in non-equilibrium thermodynamic parameters were evaluated by applying Eyring’s analyses on the data from Arrhenius plots.

Article Snippet: The recombinant envelope (E) protein (MBS143155) was originally cloned from JEV genotype III (Kamiyama strain) and obtained commercially from MyBioSource, San Diego, CA, USA.

Techniques: Binding Assay, Recombinant, Injection, Generated, Software