Sensor chip cap

Manufactured by GE Healthcare

Sourced in United States

The Sensor Chip CAP is a laboratory equipment product from GE Healthcare. It functions as a sensor chip for use in various analytical techniques. The core purpose of the Sensor Chip CAP is to facilitate data collection and analysis in a laboratory setting.

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Sensor chips (2 citations) Series S CAP sensor chip (2 citations)

8 protocols using sensor chip cap

Binding Affinity of KLK4 Inhibitory Peptide

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Example 4

Binding Affinity of KLK4 Inhibitory Peptide

Surface plasmon resonance analysis was performed using BIAcore T200 (GE healthcare) to measure the binding affinity of KLK4 inhibitory peptides by single cycle kinetics. The complementary strand of DNA of the streptavidin conjugate was captured by hybridization to Sensor Chip CAP (GE healthcare) on which the single-stranded DNA was immobilized. Next, approximately 5 RU of KLK4 biotinylated with EZ-Link NHS-PEG4-Biotin (Thermo Fisher Science) was captured at a flow rate of 10 μL/min and immobilized. Thereafter, three-fold serially diluted KLK4 inhibitory peptide (0.08 to 20 nM) with HBS-EP was added as an analyte at a flow rate of 10 μL/min. Analysis was performed using BIAcore T 200 Evaluation software (version 2.0), and k_onand k_offwere calculated using simple one-to-one Langmuir binding model. The equilibrium constant K_Dwas calculated as a k_off/k_onratio. By regenerating Sensor Chip CAP using a regeneration buffer attached to Biotin CAPture Kit (GE healthcare) and repeatedly having biotinylated KLK4 captured, multiple KLK4 inhibitory peptides were measured. All of the three measured KLK4 inhibitory peptides showed a K_Dvalue of less than 1 nM, showing that their binding is very strong (FIG. 5).

US11208467B2. Peptides inhibiting KLK1, KLK4, or KLK4 and KLK8 (2021-12-28). Daiichi Sankyo Company, Limited [JP]. Inventors: Daisuke Nishimiya [JP], Masakazu Tamura [JP].

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Measuring KLK4 Inhibitory Peptide Binding

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Example 4

Binding Affinity of KLK4 Inhibitory Peptide

US11845786B2. Peptides inhibiting KLK1, KLK4, or KLK4 and KLK8 (2023-12-19). Daiichi Sankyo Company, Limited [JP]. Inventors: Daisuke Nishimiya [JP], Masakazu Tamura [JP].

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Kinetic Analysis of KLK4 Inhibitor Binding

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SPR was measured using a BIAcore T200 (GE healthcare) with HBS-EP running buffer (10 mM HEPES, 150 mM NaCl, 3 mM EDTA, 0.05% (v/v) Surfactant P20, pH 7.4). Streptavidin conjugated DNA was captured on a Sensor Chip CAP (GE healthcare), followed by immobilization of biotinylated KLK4 on its chip at approximately 5 response units (RU). KLK4 inhibitors were subsequently captured by injection of varying concentrations (0.08–20 nM) of KLK4 inhibitors diluted with HBS-EP running buffer for 5 min at a flow of 10 μL/min, and then dissociation measured for 60–360 min with buffer flow. The signal of reference cells was subtracted from the measurements. The kinetic data of the interaction were evaluated with a global fit using BIAcore T200 evaluation software. Reference surface and chip regeneration were performed with regeneration buffer from the Biotin capture kit (GE healthcare).

Nishimiya D., Kawaguchi Y., Kodama S., Nasu H., Yano H., Yamaguchi A., Tamura M, & Hashimoto R. (2019). A protein scaffold, engineered SPINK2, for generation of inhibitors with high affinity and specificity against target proteases. Scientific Reports, 9, 11436.

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Studying PfRH5FL-mAb Binding Kinetics

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Experiments were performed at 37°C in SPR running buffer (PBS + 0.005% Polysorbate-20, GE Healthcare) using a Sensor chip CAP (GE Healthcare). The whole experiment was run at a flow rate of 5 μL/min. Approximately 1500 RU of CAP reagent (GE Healthcare) was captured on Fc 1 and Fc 2. On Fc 1, approximately 500 RU of a biotinylated control CD4d3+4-tagged protein was immobilized. On Fc 2, each experiment consisted of capturing 1500 RU of CAP reagent in an 80 s injection followed by approximately 1800 RU of PfP113Nt in an 80 s injection at a concentration of 20 μg/mL. After this, PfRH5FL-mAb complex (both at 1 μM) was flowed over Fc 1 and Fc 2. Flow cell 2 was regenerated between experiments in a 110 s injection of 6 M guanidine + 250 mM NaOH, as per the manufacturer’s instructions.

Alanine D.G., Quinkert D., Kumarasingha R., Mehmood S., Donnellan F.R., Minkah N.K., Dadonaite B., Diouf A., Galaway F., Silk S.E., Jamwal A., Marshall J.M., Miura K., Foquet L., Elias S.C., Labbé G.M., Douglas A.D., Jin J., Payne R.O., Illingworth J.J., Pattinson D.J., Pulido D., Williams B.G., de Jongh W.A., Wright G.J., Kappe S.H., Robinson C.V., Long C.A., Crabb B.S., Gilson P.R., Higgins M.K, & Draper S.J. (2019). Human Antibodies that Slow Erythrocyte Invasion Potentiate Malaria-Neutralizing Antibodies. Cell, 178(1), 216-228.e21.

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Real-time Binding Kinetics of P1 and EF-2

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The real time measurement of the interaction between P1 and PhoEF-2-GMPPCP or PhoEF-2-GDP was performed using a BIACORE 3000 biosensor system (GE Healthcare) at 37°C. Firstly, all samples were dialyzed by buffer F (10 mM HEPES, 150 mM NaCl, 100 μM MgCl₂, 0.005% polyoxyethylene sorbitan monolaurate, pH 7.4) and the buffer was used as the running buffer at the flow rate of 50 μl/min. Biotinylation using NHS-amine coupling on amino group of P1 via PEG linker was carried out using EZ-Link NHS-PEG₄-Biotin (Thermo Scientific). A sensor chip CAP (GE Healthcare) was used for the immobilization of biotinylated P1. PhoEF-2-GMPPCP and PhoEF-2-GDP was injected over the immobilized P1. The binding response at each concentration was calculated by subtracting the equilibrium response measured in the control flow cell from that in the P1 flow cell. β-2-microglobulin was used as negative control. Each resonance unit was fitted to simple 1:1 Langmuir binding model (A + B ↔ AB) using least square minimization to calculate affinity constants (K_D).

Tanzawa T., Kato K., Girodat D., Ose T., Kumakura Y., Wieden H.J., Uchiumi T., Tanaka I, & Yao M. (2018). The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion. Nucleic Acids Research, 46(6), 3232-3244.

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Biacore-based Antibody-IgE Binding

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The binding affinity of antibody candidates to IgE was evaluated by Biacore 8K (GE Healthcare, MA, USA) instrument. The Biotin CAPture reagent was captured on Sensor Chip CAP (GE Healthcare, MA, USA), followed by capturing 2 μg/ml of biotinylated full length human IgE (Biotin-FL hIgE, Abbiotec, CA, USA) with a flow rate of 10 μl/min for 60 s. Kinetic measurements were executed by injecting serially diluted antibodies with a flow rate of 30 μl/min for 180 s, followed by measuring dissociation for 400 s. The data was globally ﬁtted using a 1:1 binding model. The K_D value was evaluated by Biacore Evaluation software (GE Healthcare, MA, USA).

Liu P., Pan Z., Gu C., Cao X., Liu X., Zhang J., Xiao Z., Wang X., Guo H., Ju D, & Deng S.J. (2020). An Omalizumab Biobetter Antibody With Improved Stability and Efficacy for the Treatment of Allergic Diseases. Frontiers in Immunology, 11, 596908.

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Biolayer Interferometry Analysis of TNF-α Binding

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The Biotin CAPture Kit, including Sensor Chip CAP, Biotin CAPture reagent and regeneration solutions, Sensor Chip PEG, Recombinant MabSelect™ SuRe™ ligand, anti-TNF-α antibody, amine coupling kit and PBS-P+ Buffer 10× (0.2 M phosphate buffer with 27 mM KCl, 1.37 M NaCl and 0.5% Surfactant P20 (Tween 20)) were from GE Healthcare. Recombinant biotinylated human TNF-α (Val 77 - Leu 233) was from ACRO Biosystems(Beijing, China), recombinant human TNF receptor I protein was from Abcam (Cambridge, United Kingdom), recombinant human FcγRIIIa Val 158 and FcγRI expressed in CHO cells were kind gifts from Boehringer-Ingelheim, and bovine serum albumin (BSA) was from Sigma-Aldrich (Stockholm, Sweden).

Karlsson R., Fridh V, & Frostell Å. (2017). Surrogate potency assays: Comparison of binding profiles complements dose response curves for unambiguous assessment of relative potencies. Journal of Pharmaceutical Analysis, 8(2), 138-146.

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LRP1-FVIII Binding Kinetics Analysis

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Recombinant cluster II of LRP1 was generated as described 30. (and Marakasova et al., under preparation). The protein was biotinylated using EZ-Link Sulfo-NHS-Biotin (Thermo Fisher Scientific) and purified by Zeba Spin Desalting Columns, 7 K MWCO (Thermo Fisher Scientific). Binding assays were performed in HBS-P/Ca buffer at room temperature using a Biacore T200 instrument (GE Healthcare) as follows. Using a Biotin CAPture Kit, Series S (GE Healthcare), the biotinylated LRP1 cluster II (60 nM) was captured by preimmobilized streptavidinoligonucleotide in flow cells 1 and 2 on a sensor chip CAP (GE Healthcare). FVIII TP , FVIII FT , or FVIII EL (3.8-30 nM) in HBS-P/Ca buffer was injected over the chip with captured protein. Association and dissociation were recorded at a flow rate of 30 μL/min for 2 and 1 min, respectively, for four sets of repeats by increasing concentration of FVIII analyte.

Chun H., Pettersson J.R., Shestopal S.A., Wu W.W., Marakasova E.S., Olivares P., Surov S.S., Ovanesov M.V., Shen R.F, & Sarafanov A.G. (2021). Characterization of protein unable to bind von Willebrand factor in recombinant factor VIII products. Journal of thrombosis and haemostasis : JTH, 19(4).

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