Biacore 3000

Manufactured by Cytiva

Sourced in Sweden, United States

The Biacore 3000 is a label-free interaction analysis system that allows real-time monitoring of biomolecular interactions. It is designed to provide quantitative data on affinity, kinetics, and specificity of molecular interactions.

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Lab products found in correlation

Biaevaluation 4, by Cytiva (10 mentions) Cm5 sensor chip, by Cytiva (10 mentions) Cm5 chip, by GE Healthcare (5 mentions) Hbs ep buffer, by Cytiva (4 mentions) Cms chip, by Cytiva (3 mentions) Biaevaluation program, by Cytiva (3 mentions) Biaevaluation software, by GE Healthcare (3 mentions) Surfactant p20, by Cytiva (3 mentions) Biaevaluation software, by Cytiva (3 mentions) Amine coupling kit, by Cytiva (3 mentions) Protein a sensor chip, by Cytiva (3 mentions) Streptavidin sa sensor chips, by Cytiva (3 mentions) Carboxylated dextran cm5 chips, by Cytiva (2 mentions) Neutravidin, by Thermo Fisher Scientific (2 mentions) Cm sensor chip, by GE Healthcare (2 mentions) Biacore 3000, by GE Healthcare (2 mentions) Mouse and human hb, by Merck Group (2 mentions) Mouse hp, by MyBioSource (2 mentions) Human hp1 1, by Merck Group (2 mentions) L1 chip, by Cytiva (2 mentions)

Spelling variants of this product

BIAcore 3000 system (26 citations) BIAcore 3000 instrument (9 citations) Biacore 3000 Evaluation Software (4 citations) BIAcore 3000 SPR system (3 citations) BIAcore 3000 biosensor (2 citations) Biacore 3000 optical (2 citations)

169 protocols using biacore 3000

Determining Antibody-Antigen Affinity by SPR

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Example 10

Affinity of antibodies and antigen-binding fragments thereof described herein for to target protein can be assessed using conventional techniques such as, for example, surface plasmon resonance (SPR; Biacore).

Affinity constants for the binding of the various selected antibodies and antigen-binding fragments to target protein are determined by SPR using, for example, a BIAcore™ 3000 analytical system equipped with a CM5 sensor chip (BIAcore AB). The selected antibodies or antigen-binding fragments are covalently coupled to the CM5 sensor chip up to 1500 resonance units (using a concentration of 10 μg/mL in 10 mM acetate buffer and pH appropriate for the specific selected antibody or antigen-binding fragment tested). Target protein is injected (40 μL) at concentrations between 5 and 250 nM at a flow rate of 30 μL/min. Ten microliters of a 10 mM HCl solution is used to regenerate the chip after each cycle. Association and dissociation rate constants are calculated with the software of the BIAcore™ 3000 (Langmuir binding model).

US10982258B2. Methods of sequencing, determining, pairing, and validating therapeutic agents and disease specific antigens (2021-04-20). AbVitro LLC [US]. Inventors: Francois Vigneault [US], Adrian Wrangham Briggs [US], Christopher Ryan Clouser [US], Stephen Jacob Goldfless [US], Sonia Timberlake [US].

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Characterization of Viral Protein Interactions

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Recombinant HIV proteins gp120_ADA (product# 1081) and Tat_1-86 (product# 1002-2) were purchased from ImmunoDiagnostics, Inc. (Woburn, MA, USA). Heparin sodium salt from intestinal mucosa (CAS Number: 9041-08-1), dextran sulfate sodium salt from Leuconostoc spp. (CAS Number: 9004-54-0), and papain (CAS Number: 9001-73-4) were purchased from Sigma Aldrich (Saint Louis, MO, USA). Sensor SA chips were purchased from GE healthcare (Uppsala, Sweden). DEAE was purchased from Santa Cruz Biotech (Santa Cruz, CA, USA). SPR measurements were performed on a BIAcore 3000 operated using BIAcore 3000 control and BIAevaluation software (version 4.0.1). The marine organisms red alga B. occidentalis, and the sea urchin L. variegatus were collected and identified as previously described [27 (link),28 (link)].

Pomin V.H., Mahdi F., Jin W., Zhang F., Linhardt R.J, & Paris J.J. (2021). Red Algal Sulfated Galactan Binds and Protects Neural Cells from HIV-1 gp120 and Tat. Pharmaceuticals, 14(8), 714.

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Quantifying TIM-3-Galectin-9 Interactions

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Surface plasmon resonance (SPR) analysis of TIM-3—PS interactions in the presence of Gal-9 was performed with a Biacore 3000 instrument, as described^{74 (link)}. Lipid vesicles containing 100% DOPC or 20% DOPS were immobilized by flowing extruded lipid vesicles across an L1 sensorchip (Cytiva). Protein solutions containing a fixed concentration of TIM-3 (6 µM) with 1 mM CaCl2 and two-fold serially diluted wildtype or mutant ssGal9 flowed across lipids immobilized on the sensorchip. Resonance units detected by the Biacore 3000 were corrected for background (100% DOPC) binding and were plotted as a function of Gal-9 concentration. The dissociation kinetics were determined with GraphPad Prism using a nonlinear regression model with the dissociation one phase exponential decay equation Y = (Y0−NS)*exp(−K*X) + NS where Y0 is the binding at time zero, NS is nonspecific binding at infinite times, and K is equivalent to the rate constant for the dissociation of the protein–ligand complex, k_off.

Chongsaritsinsuk J., Steigmeyer A.D., Mahoney K.E., Rosenfeld M.A., Lucas T.M., Smith C.M., Li A., Ince D., Kearns F.L., Battison A.S., Hollenhorst M.A., Judy Shon D., Tiemeyer K.H., Attah V., Kwon C., Bertozzi C.R., Ferracane M.J., Lemmon M.A., Amaro R.E, & Malaker S.A. (2023). Glycoproteomic landscape and structural dynamics of TIM family immune checkpoints enabled by mucinase SmE. Nature Communications, 14, 6169.

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Heparin-Antithrombin III Binding Kinetics

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Porcine mucosal heparin (~16 kDa) was from Celsus Laboratories, (Cincinnati, OH). Human antithrombin III (AT III) was from Haematologic Technologies (Essex Junction, Vermont). FGF1 and FGF2 were generously provided by Amgen (Thousand Oaks, CA). GE Healthcare Bio-Sciences AB (Uppsala, Sweden) was the source of the SA sensor chips. A BIAcore 3000, running under BIAcore 3000 control and Version 4.0.1 BIAevaluation software, was used for SPR measurements.

Zhao J., Kong Y., Zhang F, & Linhardt R.J. (2018). Impact of Temperature on Heparin and Protein Interactions. Biochemistry & physiology, 7(2), 241.

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Heparin-Antithrombin III Binding Kinetics

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Zhao J., Kong Y., Zhang F, & Linhardt R.J. (2018). Impact of Temperature on Heparin and Protein Interactions. Biochemistry & physiology, 7(2), 241.

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SARS-CoV-2 Spike Protein Interaction with Sulfated Glycans

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Fourteen sulfated glycans (Table 1) were collected from their manufacturers in Dr. Fareed’s Lab. SARS-CoV-2 S-protein RBD wild type (WT) and N501Y were expressed in Expi293F cells provided by the Bates Lab, University of Mississippi Medical Center. SARS-CoV-2 S-protein RBD mutants (related to Delta variants of SARS-CoV-2) were purchased from Sino Biological US Inc. (Wayne, PA, USA). SARS-CoV-2 pseudoviral particles (WT and Delta variant) were prepared in Tandon’s Lab as previously described [27 (link)]. Sensor SA chips were from Cytiva (Uppsala, Sweden). SPR measurements were performed on a BIAcore 3000 operated using BIAcore 3000 or T200 SPR (Cytiva, Uppsala, Sweden). The cell line HEK293T was purchased from American Type Culture Collection (ATCC, Manassas, VA, USA).

Zhang F., He P., Rodrigues A.L., Jeske W., Tandon R., Bates J.T., Bierdeman M.A., Fareed J., Dordick J, & Linhardt R.J. (2022). Potential Anti-SARS-CoV-2 Activity of Pentosan Polysulfate and Mucopolysaccharide Polysulfate. Pharmaceuticals, 15(2), 258.

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SPR Analysis of Acetylcholine Receptor Binding

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Example 4

A surface plasmon resonance (SPR) experiment was progressed using a biosensor chip to compare binding forces for acetylcholine receptors of S6_1 (SEQ ID NO: 23, WTWKGKGTLNR), i.e., discovered peptides and S6_1_C6 (SEQ ID NO: 31, KGTLNR), i.e., a deleted form, and Synake and Vialox, i.e., a positive control group (Biacore 3000, Biacore AB, Uppsala, Sweden).

After fixing selected acetylcholine receptor proteins to a CMS chip (Biacore) using EDC/NHS, association and dissociation were observed for up to 500 seconds. A binding force comparing experiment was carried out under observation conditions of a running buffer of 20 mM Tris (pH 7.4), a speed of 30 [Figure (not displayed)]/min, and a peptide concentration of 10 μM (Synake, Vialox, S6_1, S6_1_C6). Results of the binding force comparing experiment are shown in FIG. 6.

US11472840B2. Acetylcholine receptor-binding peptide (2022-10-18). AMICOGEN, INC. [KR]. Inventors: Sung Hyun Kim [KR], Won Il Choi [KR], Yong Chul Shin [KR], Jeung Hoon Lee [KR], Young Sung Yun [KR], Jin Hwa Kim [KR].

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Acetylcholine Receptor Binding Assay

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Example 3

S6_1 (SEQ ID NO:23, WTWKGKGTLNR), S6_2 (SEQ ID NO: 2 4, WTWKGRKSLLR), S6_3 (SEQ ID NO: 25, WTWKGEDKGKN), S6_4 (SEQ ID NO: 26, WTWKGRDKLQM) showing sequence similarities through multiple alignments among the peptides in Table 2 were synthesized.

A surface plasmon resonance (SPR) experiment was progressed using a biosensor chip to compare binding forces for the acetylcholine receptors thereof (Biacore 3000, Biacore AB, Uppsala, Sweden). After fixing selected acetylcholine receptor proteins to a CMS chip (Biacore) using EDC/NHS, association and dissociation were observed for up to 500 seconds. A binding force comparing experiment was carried out under observation conditions of a running buffer of 20 mM Tris (pH 7.4), a speed of 30 [Figure (not displayed)]/min, and a peptide concentration of 10 μM (S6_1, S6_2, S6_3, S6_4). Results of the binding force comparing experiment are shown in FIG. 5.

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Apolipoprotein-Phospholipid Binding Kinetics

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Binding kinetics of PIP2 with different apolipoproteins were analyzed using a Biacore3000 instrument. Either biotinylated apoA1 or biotinylated PIP2 was immobilized on streptavidin sensor chips. For comparing binding kinetics of PIP2 with apoA1, apoA2 and apoE, these proteins were immobilized by covalent coupling on a CM5 sensor chip.

Gulshan K., Brubaker G., Conger H., Wang S., Zhang R., Hazen S.L, & Smith J.D. (2016). PI(4,5)P2 is translocated by ABCA1 to the cell surface where it mediates apolipoprotein A1 binding and nascent HDL assembly, and it is carried on HDL. Circulation research, 119(7), 827-838.

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Real-time Monitoring of RppH-DapF Interaction

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Real-time interaction of RppH with DapF was monitored by Surface Plasmon Resonance (SPR) detection using a BIAcore 3000 (BIAcore AB) instrument as previously described with some modifications (27 (link)–29 (link)). RppH was immobilized onto the carboxymethylated dextran surface of a CM5 sensor chip. RppH (100 μl, 5 μg/ml) in coupling buffer (10 mM sodium acetate, pH 5.0) was flowed over the sensor chip at 5 μl/min to couple the proteins to the matrix by an N-hydroxysuccinimide/N-ethyl-N′(3-diethylaminopropyl)-carbodiimide reaction (80 μl of mix). Assuming that 1000 resonance units correspond to a surface concentration of 1 ng/mm², RppH was immobilized to a surface concentration of 0.7 ng/mm². The standard running buffer was 10-mM 4-2-hydroxyethyl-1-piperazineethanesulfonic acid (HEPES) (pH 7.2), 150 mM NaCl, 10 mM KCl, 1 mM MgCl₂ and 0.5 mM ethylenediaminetetraacetic acid, and all reagents were introduced at a flow rate of 10 μl/min. The sensor surface was regenerated between assays by using the standard running buffer at a flow rate of 100 μl/min for 10 min to remove bound analytes.

Lee C.R., Kim M., Park Y.H., Kim Y.R, & Seok Y.J. (2014). RppH-dependent pyrophosphohydrolysis of mRNAs is regulated by direct interaction with DapF in Escherichia coli. Nucleic Acids Research, 42(20), 12746-12757.

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