bio rad system software Search Results


image labtm software version 6 0 1  (Bio-Rad)
99
Bio-Rad image labtm software version 6 0 1
Image Labtm Software Version 6 0 1, supplied by Bio-Rad, 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/product/bio+rad+system+software/10__20517_slash_cdr__2025__175-108-5-10?v=Bio-Rad
Average 99 stars, based on 1 article reviews
image labtm software version 6 0 1 - by Bioz Stars, 2026-08
99/100 stars
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microplate manager  (Bio-Rad)
99
Bio-Rad microplate manager
Microplate Manager, supplied by Bio-Rad, 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/product/bio+rad+system+software/10__3390_slash_ruminants6020035-83-18-20?v=Bio-Rad
Average 99 stars, based on 1 article reviews
microplate manager - by Bioz Stars, 2026-08
99/100 stars
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cfx96 real time system c1000 thermal cycler  (Bio-Rad)
94
Bio-Rad cfx96 real time system c1000 thermal cycler
Cfx96 Real Time System C1000 Thermal Cycler, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/bio+rad+system+software/pm33106338-110-8-15?v=Bio-Rad
Average 94 stars, based on 1 article reviews
cfx96 real time system c1000 thermal cycler - by Bioz Stars, 2026-08
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imagelab software version 5 2 1  (Bio-Rad)
99
Bio-Rad imagelab software version 5 2 1
Imagelab Software Version 5 2 1, supplied by Bio-Rad, 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/product/bio+rad+system+software/bio_rxiv__706259-323-4-8?v=Bio-Rad
Average 99 stars, based on 1 article reviews
imagelab software version 5 2 1 - by Bioz Stars, 2026-08
99/100 stars
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opticon monitor software version 3 1  (Bio-Rad)
99
Bio-Rad opticon monitor software version 3 1
Opticon Monitor Software Version 3 1, supplied by Bio-Rad, 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/product/bio+rad+system+software/10__1007_slash_s13157___018___1001___1-106-16-21?v=Bio-Rad
Average 99 stars, based on 1 article reviews
opticon monitor software version 3 1 - by Bioz Stars, 2026-08
99/100 stars
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bio rad proteon manager software  (Bio-Rad)
96
Bio-Rad bio rad proteon manager software
FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a <t>ProteOn</t> system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.
Bio Rad Proteon Manager Software, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/bio+rad+system+software/10__1128_slash_jvi__05406___11-137-14-14?v=Bio-Rad
Average 96 stars, based on 1 article reviews
bio rad proteon manager software - by Bioz Stars, 2026-08
96/100 stars
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precision melt analysis software pmas  (Bio-Rad)
96
Bio-Rad precision melt analysis software pmas
FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a <t>ProteOn</t> system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.
Precision Melt Analysis Software Pmas, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/bio+rad+system+software/pm36309432-108-6-11?v=Bio-Rad
Average 96 stars, based on 1 article reviews
precision melt analysis software pmas - by Bioz Stars, 2026-08
96/100 stars
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cfx maestrotm software version 2 2  (Bio-Rad)
98
Bio-Rad cfx maestrotm software version 2 2
FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a <t>ProteOn</t> system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.
Cfx Maestrotm Software Version 2 2, supplied by Bio-Rad, 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/product/bio+rad+system+software/pm37762153-229-11-16?v=Bio-Rad
Average 98 stars, based on 1 article reviews
cfx maestrotm software version 2 2 - by Bioz Stars, 2026-08
98/100 stars
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bio plexmanager 2 0 software  (Bio-Rad)
95
Bio-Rad bio plexmanager 2 0 software
FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a <t>ProteOn</t> system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.
Bio Plexmanager 2 0 Software, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/bio+rad+system+software/pm23236021-93-19-22?v=Bio-Rad
Average 95 stars, based on 1 article reviews
bio plexmanager 2 0 software - by Bioz Stars, 2026-08
95/100 stars
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image lab touch software v2 4  (Bio-Rad)
99
Bio-Rad image lab touch software v2 4
FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a <t>ProteOn</t> system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.
Image Lab Touch Software V2 4, supplied by Bio-Rad, 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/product/bio+rad+system+software/pmc08748497-319-11-16?v=Bio-Rad
Average 99 stars, based on 1 article reviews
image lab touch software v2 4 - by Bioz Stars, 2026-08
99/100 stars
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iqtm5 optical system software  (Bio-Rad)
99
Bio-Rad iqtm5 optical system software
FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a <t>ProteOn</t> system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.
Iqtm5 Optical System Software, supplied by Bio-Rad, 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/product/bio+rad+system+software/pmc06893788-94-14-18?v=Bio-Rad
Average 99 stars, based on 1 article reviews
iqtm5 optical system software - by Bioz Stars, 2026-08
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bio plex data pro software  (Bio-Rad)
95
Bio-Rad bio plex data pro software
FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a <t>ProteOn</t> system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.
Bio Plex Data Pro Software, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 95 stars, based on 1 article reviews
bio plex data pro software - by Bioz Stars, 2026-08
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Image Search Results


FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a ProteOn system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.

Journal: Journal of Virology

Article Title: H5N1 Virus-Like Particle Vaccine Elicits Cross-Reactive Neutralizing Antibodies That Preferentially Bind to the Oligomeric Form of Influenza Virus Hemagglutinin in Humans

doi: 10.1128/jvi.05406-11

Figure Lengend Snippet: FIG. 2. Characterization of bacterially expressed and purified H5N1 HA proteins. (A and B) Characterization of purified H5N1 HA proteins from E. coli by Superdex S-200 gel filtration chromatography. Purified H5N1 HA1 proteins with an intact N terminus (positions 1 to 320) (A) and HA1 with an N-terminal deletion (28 to 320) (B) were subjected to gel filtration. The panels show superimposed elution profiles of purified HA1 proteins (red lines) overlaid with calibration standards (gray lines). The elution volumes of protein species are shown in parentheses. (C and D) Steady-state binding equilibrium analysis of conformation-dependent human H5N1 neutralizing MAbs FLD21.40 (C) and FLA3.14 (D) at 10 g/ml to purified bacterially expressed H5N1 HA1 proteins immobilized on a sensor chip through the free amine group and on a blank flow cell, free of peptide. Binding was recorded using a ProteOn system surface plasmon resonance biosensor instrument (Bio-Rad Labs, Hercules, CA). (E) Agglutination of human RBCs by properly folded oligomeric H5N1 rHA1(1-320) protein and its monomeric H5N1 rHA1(28-320) counterpart along with rgH5N1 virus. Serial dilutions of purified HA1 proteins were mixed with washed RBCs, and hemagglutination was read after 30 min at room temperature. Reassorted virus rgH5N1xPR8 (2:6) A/Vietnam/1203/2004 (clade 1) was used as a positive control.

Article Snippet: Binding kinetics for the selected human vaccine sera and data analyses were calculated using Bio-Rad ProteOn manager software (version 2.0.1).

Techniques: Chromatography, Binding Assay, SPR Assay, Agglutination, Virus, Positive Control