Ni nta sensors

Manufactured by Molecular Devices

Sourced in United States, China

Ni-NTA sensors are a type of analytical tool used for the detection and measurement of specific biomolecules in a sample. They utilize nickel-nitrilotriacetic acid (Ni-NTA) technology to selectively capture and immobilize proteins or other molecules of interest, allowing for their analysis. The core function of Ni-NTA sensors is to facilitate the study and characterization of biomolecular interactions and properties.

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Lab products found in correlation

Blitz system, by Molecular Devices (1 mentions) Ethylenediaminetetraacetic acid, by Beyotime (1 mentions) Acetonitrile, by Thermo Fisher Scientific (1 mentions) Fetal bovine serum (fbs), by Lonsera (1 mentions) Gapdh af7021, by Affinity Biosciences (1 mentions) P38mapk d13e1, by Cell Signaling Technology (1 mentions) Ni nta beads 6ff, by Smart-Lifesciences (1 mentions) Triethylammonium bicarbonate teab, by Merck Group (1 mentions) Tmt kit, by Thermo Fisher Scientific (1 mentions) Endofree plasmid midi kit, by CWBIO (1 mentions) Dulbecco s modified eagle s medium dmem, by Merck Group (1 mentions) Fastpure gel dna extraction mini kit, by Vazyme (1 mentions) Bca protein assay kit, by Beyotime (1 mentions) Phosstop phosphatase inhibitor, by Roche (1 mentions) Trypsin edta, by Beyotime (1 mentions) Octet k2 system, by Molecular Devices (1 mentions) 96 well flat bottom black plate, by Greiner (1 mentions) Octet red96 platform, by Molecular Devices (1 mentions) Data analysis software 9, by Molecular Devices (1 mentions) Protein g sensors, by Molecular Devices (1 mentions)

Close spelling variants of this product

Ni-NTA (8 citations) NTA sensor (2 citations)

5 protocols using ni nta sensors

Cps2D-SpAdK Binding Kinetics Assay

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BLI experiments were performed using a Blitz system (ForteBio, CA, USA). His₆-Cps2D WT or 3Y3E mutant protein (1 μM) were immobilized on Ni-NTA sensors (ForteBio, CA, USA). Binding of SpAdK was monitored by adding various concentrations of glutathione S-transferase (GST)-SpAdK (2.5–50 μM) in buffer D (250 mM NaCl, 50 mM Tris-HCl, pH 7.5, and 1 mM DTT) in the absence or presence of 5 mM Mg-ATP. BLI experiments with Cps2D GK-AA and GK-AA/3Y3E were similarly performed in buffer D. GST protein was used as a negative control, and background signals from GST and sensors were subtracted before binding analysis. The experiments were repeated at least twice. K_d values were determined using steady-state analysis with GraphPad Prism (GraphPad Software Inc, CA, USA).

Ghosh P., Luong T.T., Shah M., Thach T.T., Choi S., Lee S, & Rhee D.K. (2018). Adenylate kinase potentiates the capsular polysaccharide by modulating Cps2D in Streptococcus pneumoniae D39. Experimental & Molecular Medicine, 50(9), 116.

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Activation of p38 MAPK Pathway

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Reagents: Dulbecco's modified eagle's medium (DMEM) (Sigma-Aldrich, MO, USA); fetal bovine serum (FBS) (Lonsera, UY, South America); p38 mitogen activated protein kinase (p38 MAPK) (D13E1) (8690, Cell Signaling Technology, MA, USA); phospho-p38 MAPK (P-p38 MAPK) (Thr180/Tyr182) (4631, Cell Signaling Technology, MA, USA); GAPDH (AF7021, Affinity Biosciences, Beijing, China); horseradish peroxidase (HRP)-conjugated anti-rabbit IgG (S0001, Affinity Biosciences, Beijing, China); phosSTOP phosphatase inhibitor (Roche, Basel, Switzerland); GC-rich PCR master mix (Sangon Biotech, Shanghai, China); acetonitrile (Fisher Chemical, Fairlawn, USA); triethylammonium bicarbonate (TEAB) (Sigma-Aldrich, MO, USA); Escherichia coli BL21(DE3) competent cells (Solarbio, Beijing, China); Ni NTA Beads 6FF (Smart-Lifesciences, Jiangsu, China); BCA protein assay kit (Beyotime, Shanghai, China); endofree plasmid midi kit (Cwbiotech, Beijing, China); fastpure gel DNA extraction mini kit (Vazyme Biotech, Jiangsu, China); Ni-NTA sensors (ForteBio, CA, USA); tandem mass tagging (TMT) Kit (Thermo, Waltham, USA). Ethylene diamine tetraacetic acid (EDTA), 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (MTT) and trypsin-EDTA (TE) were obtained from Beyotime Technology (Shanghai, China).

Lu C., Fan L., Zhang P.F., Tao W.W., Yang C.B., Shang E.X., Chen F.Y., Che C.T., Cheng H.B., Duan J.A, & Zhao M. (2021). A novel P38α MAPK activator Bruceine A exhibits potent anti-pancreatic cancer activity. Computational and Structural Biotechnology Journal, 19, 3437-3450.

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In vitro Binding Assays of PirC

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In vitro binding studies were done by BLI using Octet K2 system (FortéBio) as described previously (10 (link)). In the first step, P_II-His₈ (400 nM, trimeric) or PGAM-His₆ (500 nM) was immobilized on Ni-NTA sensors (FortéBio), followed by a 60-s baseline measurement. For the binding of PirC, the biosensors were dipped into the PirC solution for 180 s (association), with concentrations ranging between 9.375 nM to 1,500 nM. In P_II-binding studies, effector molecules ADP, ATP, or 2-OG were added to the binding buffer as indicated and in PGAM binding assays, 2PG or 3 PGA. Finally, the complexes were allowed to dissociate for 300 s. For each binding experiment, a negative control without an interaction partner was performed in parallel. The response in equilibrium (R_eq) was calculated using the data analysis software of the Octet System. To calculate the dissociation constant K_D, the concentration versus R_eq plots were made for each set of experiments.

Orthwein T., Scholl J., Spät P., Lucius S., Koch M., Macek B., Hagemann M, & Forchhammer K. (2021). The novel PII-interactor PirC identifies phosphoglycerate mutase as key control point of carbon storage metabolism in cyanobacteria. Proceedings of the National Academy of Sciences of the United States of America, 118(6), e2019988118.

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Kinetic Analysis of EBOV GP Binding

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Kinetics experiments were performed using the ForteBio Octet Red96 platform. All data was collected at 25°C with orbital shaking at 1,000 rpm in 200 μL in 96-well black flat bottom plates (Greiner Bio-one). For CA45 IgG kinetics, reagents were diluted in 1X kinetics buffer (1X PBS, 0.01% BSA and 0.002% Tween-20) supplied by ForteBio. Protein G sensors (ForteBio) were equilibrated for 10 minutes in 1X kinetics buffer prior to loading with 5 μg/mL of CA45 for 2 minutes. After the loading step, a 30-second baseline in 1X kinetics buffer was established before association with a range of concentrations of GPΔTM for EBOV, SUDV, BDBV, or RESTV or EBOV GP_CL for 5 minutes. Following CA45 association with GP, there was a 10-minute of dissociation step in kinetics buffer. For CA45 Fab kinetics, all reagents were diluted in 100 mM sodium phosphate, 150 mM NaCl, 0.02% Tween-20 pH 6.0 to reduce non-specific binding. His-tagged EBOV GPΔTM was loaded onto pre-wet Ni-NTA sensors (ForteBio) for 120 seconds, followed by a 60-second baseline and then association with a range of CA45 Fab concentrations. The association step was followed by a 10-minute dissociation step. For all experiments, a reference sensor without ligand was used to account for nonspecific binding of analyte to the sensor. All data was fit globally to a 1:1 Langmuir binding model using data analysis software 9.0 (ForteBio).

Zhao X., Howell K.A., He S., Brannan J.M., Wec A.Z., Davidson E., Turner H.L., Chiang C.I., Lei L., Fels J.M., Vu H., Shulenin S., Turonis A.N., Kuehne A.I., Liu G., Ta M., Wang Y., Sundling C., Xiao Y., Spence J.S., Doranz B.J., Holtsberg F.W., Ward A.B., Chandran K., Dye J.M., Qiu X., Li Y, & Aman M.J. (2017). Immunization-elicited Broadly Protective Antibody Reveals Ebolavirus Fusion Loop as a Site of Vulnerability. Cell, 169(5), 891-904.e15.

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BLI Kinetics Assay of Anti-E-Cadherin Fabs

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BLI kinetics assays were performed on an Octet Red96 at 23°C, shaking at 1000 rpm. Protein was diluted in kinetics buffer: 50 mM Tris pH 8.0, 150 mM NaCl, 3mM CaCl2, 0.25 mg/mL BSA, 0.005% Tween-20. Ni-NTA sensors (ForteBio) were equilibrated for 60 seconds, then E-cadherin EC1-5-TwinStrep-8His was loaded onto the sensor for 180 seconds, followed by another 60 second baseline. Sensors were then immersed into a 1:3 dilution series of anti-E-cadherin Fabs in kinetics buffer until they reached desired concentrations, then dipped into empty kinetics buffer to determine off-rates. ForteBio data analysis software was used to calculate kinetics parameters such as kon, koff, and KD using a 1:1 binding global fit model. Assays were repeated at least twice with different Fab preparations to ensure consistent results. For 19A11 and 46H7, both ficin-cleaved untagged Fabs and TwinStrep tagged Fabs were tested; both showed similar affinities regardless of presence of tag (Extended Data Figure 4F).

Maker A., Bolejack M., Schecterson L., Hammerson B., Abendroth J., Edwards T.E., Staker B.L., Myler P.J., & Gumbiner B.M. (2022). Regulation of multiple dimeric states of E-cadherin by adhesion activating antibodies revealed through Cryo-EM and X-ray crystallography.

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