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Anti human fab ch1 fab2g biosensors

Manufactured by Molecular Devices
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The Anti-human Fab-CH1 (FAB2G) biosensors are laboratory equipment designed for the detection and analysis of Fab fragments, a type of antibody structure. These biosensors utilize surface plasmon resonance (SPR) technology to provide real-time, label-free monitoring of biomolecular interactions involving Fab fragments.

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Lab products found in correlation

Octet system data analysis v9, by Molecular Devices (3 mentions) Octet red instrument, by Molecular Devices (3 mentions) Prism version 8, by GraphPad (2 mentions) Octet red96 instrument, by Molecular Devices (1 mentions) Anti human igg fc capture ahc, by Molecular Devices (1 mentions)

6 protocols using anti human fab ch1 fab2g biosensors

1

Kinetic Analysis of Antibody-Antigen Binding

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An Octet RED instrument (FortéBio) was used to determine the kinetic parameters of the antibody–antigen interactions by Biolayer Interferometry. Monoclonal Fabs were loaded onto anti-human Fab-CH1 (FAB2G) biosensors (FortéBio) at a concentration of 10 μg/mL in kinetics buffer (PBS, pH 7.4, 0.01% [w/v] BSA, and 0.002% [v/v] Tween 20) until a response of 1 nanometer shift was reached. Loaded biosensors were dipped into kinetics buffer for 1 min to acquire a baseline and then moved to wells containing a series of 2-fold dilutions of BG505 SOSIP.v5.2 in kinetics buffer, starting at a 4000 nM. The trimers were allowed to associate for 180 secs before the biosensor were move back to the wells containing kinetics buffer where the baseline was acquired. Disassociation of the trimers from the Fab-loaded biosensors was recorded for 300 secs. All BLI experiments were conducted at 37°C. Kinetic parameters were calculated using the Octet System Data Analysis v9.0 (FortéBio).
Cottrell C.A., van Schooten J., Bowman C.A., Yuan M., Oyen D., Shin M., Morpurgo R., van der Woude P., van Breemen M., Torres J.L., Patel R., Gross J., Sewall L.M., Copps J., Ozorowski G., Nogal B., Sok D., Rakasz E.G., Labranche C., Vigdorovich V., Christley S., Carnathan D.G., Sather D.N., Montefiori D., Silvestri G., Burton D.R., Moore J.P., Wilson I.A., Sanders R.W., Ward A.B, & van Gils M.J. (2020). Mapping the immunogenic landscape of near-native HIV-1 envelope trimers in non-human primates. PLoS Pathogens, 16(8), e1008753.
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2

Biolayer Interferometry Assessment of Antibody-Antigen Interactions

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An Octet RED instrument (FortéBio) was used to assess antibody-antigen interactions by Biolayer Interferometry. VRC40.01 or VRC40.01_FR-H3 deletion Fabs were loaded onto anti-human Fab-CH1 (FAB2G) biosensors (FortéBio) at a concentration of 5 μg/mL in kinetics buffer (PBS, pH 7.4, 0.01% [w/v] BSA, and 0.002% [v/v] Tween 20) until a response of 0.5 nm shift was reached. Loaded biosensors were dipped into kinetics buffer for 1 min to acquire a baseline and then moved to wells containing 4 μM BG505 SOSIP.664 in kinetics buffer. The trimers were allowed to associate for 180 s before the biosensor were move back to the wells containing kinetics buffer where the baseline was acquired. Disassociation of the trimers from the Fab-loaded biosensors was recorded for 300 s. All BLI experiments were conducted at 37°C. Background subtracted results were plotted using Prism version 8.4.2 (GraphPad). For the VRC40.01 germline revertant binding assays, the biotinylated BG505 DS-SOSIP trimer (at 30 μg/ml) was captured on Streptavidin sensor tips and then dipped into the IgG antibody solution at a series of concentrations from 0.05 to 6.5 μM. The data were fitted with the Octet software Forte Data Analysis 11.
Cottrell C.A., Manne K., Kong R., Wang S., Zhou T., Chuang G.Y., Edwards R.J., Henderson R., Janowska K., Kopp M., Lin B.C., Louder M.K., Olia A.S., Rawi R., Shen C.H., Taft J.D., Torres J.L., Wu N.R., Zhang B., Doria-Rose N.A., Cohen M.S., Haynes B.F., Shapiro L., Ward A.B., Acharya P., Mascola J.R, & Kwong P.D. (2021). Structural basis of glycan276-dependent recognition by HIV-1 broadly neutralizing antibodies. Cell reports, 37(5), 109922.
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3

Kinetic Analysis of Influenza Antibodies

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CR9114 and S9-3-37 IgG at 5 μg/mL or MEDI8852, C05, and HIV PG9 Fab fragments at 20 μg/mL were loaded onto anti-human IgG Fc Capture (AHC) or anti-human Fab CH1 (FAB2G) biosensors (ForteBio, Fremont, CA, USA) in kinetics buffer (0.01% BSA + 0.002% Tween20 in 1× phosphate-buffered saline) and dipped into wells containing HAstem (135 nM or 270 nM), CLP-HAstem (250 nM or 500 nM total protein), or kinetics buffer alone using an Octet Red96 instrument (ForteBio). After loading, association was measured for 700 s, followed by dissociation for 750 s in kinetics buffer. A baseline containing kinetics buffer was subtracted from each data set, and curves were aligned on the y axis using the baseline step.
Thrane S., Aves K.L., Uddbäck I.E., Janitzek C.M., Han J., Yang Y.R., Ward A.B., Theander T.G., Nielsen M.A., Salanti A., Thomsen A.R., Christensen J.P, & Sander A.F. (2020). A Vaccine Displaying a Trimeric Influenza-A HA Stem Protein on Capsid-Like Particles Elicits Potent and Long-Lasting Protection in Mice. Vaccines, 8(3), 389.
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4

SOSIP Trimer Binding Kinetics

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Monoclonal Fabs were loaded onto anti-human Fab-CH1 (FAB2G) biosensors (FortéBio) at a concentration of 10 μg/mL in kinetics buffer (PBS, pH 7.4, 0.01% [w/v] BSA, and 0.002% [v/v] Tween 20) until a response of 1 nanometer shift was reached. Loaded biosensors were dipped into wells containing only kinetics buffer for 1 min to acquire a baseline and then moved to wells containing 2000 nM SOSIP trimer in kinetics buffer. The trimers were allowed to associate for 180 s before the biosensor were move back to the wells containing only kinetics buffer where the baseline was acquired. Disassociation of the trimers from the Fab-loaded biosensors was recorded for 300 s. All BLI experiments were conducted at 37°C and the data were processed using the Octet System Data Analysis v9.0 (FortéBio).
Rossignol E.D., Dugast A.S., Compere H., Cottrell C.A., Copps J., Lin S., Cizmeci D., Seaman M.S., Ackerman M.E., Ward A.B., Alter G, & Julg B. (2021). Mining HIV controllers for broad and functional antibodies to recognize and eliminate HIV-infected cells. Cell reports, 35(8), 109167.
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5

SOSIP Trimer Binding Kinetics

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Monoclonal Fabs were loaded onto anti-human Fab-CH1 (FAB2G) biosensors (FortéBio) at a concentration of 10 μg/mL in kinetics buffer (PBS, pH 7.4, 0.01% [w/v] BSA, and 0.002% [v/v] Tween 20) until a response of 1 nanometer shift was reached. Loaded biosensors were dipped into wells containing only kinetics buffer for 1 min to acquire a baseline and then moved to wells containing 2000 nM SOSIP trimer in kinetics buffer. The trimers were allowed to associate for 180 s before the biosensor were move back to the wells containing only kinetics buffer where the baseline was acquired. Disassociation of the trimers from the Fab-loaded biosensors was recorded for 300 s. All BLI experiments were conducted at 37°C and the data were processed using the Octet System Data Analysis v9.0 (FortéBio).
Rossignol E.D., Dugast A.S., Compere H., Cottrell C.A., Copps J., Lin S., Cizmeci D., Seaman M.S., Ackerman M.E., Ward A.B., Alter G, & Julg B. (2021). Mining HIV controllers for broad and functional antibodies to recognize and eliminate HIV-infected cells. Cell reports, 35(8), 109167.
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6

Biolayer Interferometry Assessment of Antibody-Antigen Interactions

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An Octet RED instrument (FortéBio) was used to assess antibody-antigen interactions by Biolayer Interferometry. VRC40.01 or VRC40.01_FR-H3 deletion Fabs were loaded onto anti-human Fab-CH1 (FAB2G) biosensors (FortéBio) at a concentration of 5 μg/mL in kinetics buffer (PBS, pH 7.4, 0.01% [w/v] BSA, and 0.002% [v/v] Tween 20) until a response of 0.5 nm shift was reached. Loaded biosensors were dipped into kinetics buffer for 1 min to acquire a baseline and then moved to wells containing 4 μM BG505 SOSIP.664 in kinetics buffer. The trimers were allowed to associate for 180 s before the biosensor were move back to the wells containing kinetics buffer where the baseline was acquired. Disassociation of the trimers from the Fab-loaded biosensors was recorded for 300 s. All BLI experiments were conducted at 37°C. Background subtracted results were plotted using Prism version 8.4.2 (GraphPad). For the VRC40.01 germline revertant binding assays, the biotinylated BG505 DS-SOSIP trimer (at 30 μg/ml) was captured on Streptavidin sensor tips and then dipped into the IgG antibody solution at a series of concentrations from 0.05 to 6.5 μM. The data were fitted with the Octet software Forte Data Analysis 11.
Cottrell C.A., Manne K., Kong R., Wang S., Zhou T., Chuang G.Y., Edwards R.J., Henderson R., Janowska K., Kopp M., Lin B.C., Louder M.K., Olia A.S., Rawi R., Shen C.H., Taft J.D., Torres J.L., Wu N.R., Zhang B., Doria-Rose N.A., Cohen M.S., Haynes B.F., Shapiro L., Ward A.B., Acharya P., Mascola J.R, & Kwong P.D. (2021). Structural basis of glycan276-dependent recognition by HIV-1 broadly neutralizing antibodies. Cell reports, 37(5), 109922.
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