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Neutravidin immobilized nlc proteon sensor chip

Manufactured by Bio-Rad

The NeutrAvidin-immobilized NLC ProteOn sensor chip is a lab equipment product designed for use in the ProteOn XPR36 interaction array system. The sensor chip features a NeutrAvidin surface, which is used to capture biotinylated molecules for subsequent analysis of molecular interactions.

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2 protocols using neutravidin immobilized nlc proteon sensor chip

1

Kinetic Analysis of Monoclonal Antibodies

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Biotinylated NPDP15 and NANP18 peptides were diluted (20 nM) in HEPES buffered saline (HBS) (10 mM HEPES, pH 7.4, 150 mM NaCl, 3 mM EDTA, 0.005% surfactant Tween-20). HBS was also used as running buffer. An irrelevant biotinylated 19-mer peptide was used as a control for non-specific interactions. A NeutrAvidin-immobilized NLC ProteOn sensor chip (Biorad) was pre-conditioned with an NaCl solution (1 M) and the biotinylated peptides were injected onto the chip. The monoclonal antibodies were diluted and titrated in HBS (50-16.7-5.6-1.9-0.6 nM) and injected onto chip; one channel of the chip was injected with HBS and used as reference for the analysis. All injections were made at a flow rate of 100 μl/min. Injection time and dissociation time were 240 s and 900 s, respectively. Each binding interaction of the monoclonal antibodies with the biotinylated peptides was assessed using a ProteON XPR36 instrument (Biorad) and data were processed with ProteOn Manager Software (version 3.1.0.6). Ka, Kd and KD were calculated by applying the Langmuir fit model.
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2

Kinetic Analysis of Monoclonal Antibodies

Check if the same lab product or an alternative is used in the 5 most similar protocols
Biotinylated NPDP15 and NANP18 peptides were diluted (20 nM) in HEPES buffered saline (HBS) (10 mM HEPES, pH 7.4, 150 mM NaCl, 3 mM EDTA, 0.005% surfactant Tween-20). HBS was also used as running buffer. An irrelevant biotinylated 19-mer peptide was used as a control for non-specific interactions. A NeutrAvidin-immobilized NLC ProteOn sensor chip (Biorad) was pre-conditioned with an NaCl solution (1 M) and the biotinylated peptides were injected onto the chip. The monoclonal antibodies were diluted and titrated in HBS (50-16.7-5.6-1.9-0.6 nM) and injected onto chip; one channel of the chip was injected with HBS and used as reference for the analysis. All injections were made at a flow rate of 100 μl/min. Injection time and dissociation time were 240 s and 900 s, respectively. Each binding interaction of the monoclonal antibodies with the biotinylated peptides was assessed using a ProteON XPR36 instrument (Biorad) and data were processed with ProteOn Manager Software (version 3.1.0.6). Ka, Kd and KD were calculated by applying the Langmuir fit model.
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