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Biacore 3000 spr biosensor instrument
3000 Spr Biosensor Instrument, supplied by Biacore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/3000+spr+biosensor/3000+biacore+instrument/us12624124-815-19-18
Average 86 stars, based on 1 article reviews
3000 spr biosensor instrument - by Bioz Stars, 2026-10
86/100 stars

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Related Articles

SPR Assay:

Article Title: Identification of Critical Paraoxonase 1 Residues Involved in High Density Lipoprotein Interaction
Article Snippet: Full time course kinetic determinations of k on , k off , and apparent equilibrium dissociation constants K d for rHDL interaction with rPON1 forms were determined using SPR using a BIAcore 3000 SPR biosensor (BIAcore, AB). .. Full time course kinetic determinations of k on , k off , and apparent equilibrium dissociation constants K d for rHDL interaction with rPON1 forms were determined using SPR using a BIAcore 3000 SPR biosensor (BIAcore, AB). ..

Article Title: Open-sandwich molecular imprinting: making a recognition matrix with antigen-imprinted antibody fragments.
Article Snippet: A novel antibody−polymer conjugation method termed open-sandwich molecular imprinting (OS-MIP) has been proposed to produce a specific recognition matrix in the presence of a target antigen.. The resultant carboxymethyldextran matrix conjugated with two separate antibody variable region fragments imprinted with the cognate antigen showed higher antigen-binding capacity than non-imprinted ones and was successfully used to sensitively monitor multiple antigen binding/desorption events by a surface plasmon resonance biosensor.. Furthermore, when each fragment was labeled with different fluorophores before conjugation, the fluorescence signals of the matrix made by OS-MIP clearly showed an antigen concentration dependent increase in Förster resonance energy transfer between the two dyes.

Article Title: Pathogenic Neisseria meningitidis utilizes CD147 for vascular colonization
Article Snippet: Light signal was detected with the EnVision multilabel plate reader (PerkinElmer). .. Surface plasmon resonance (SPR) experiments were carried out on a Biacore 3000 SPR biosensor (Biacore InternationalAB). ..

Article Title: Pathogenic Neisseria meningitidis utilizes CD147 for vascular colonization.
Article Snippet: .. Surface plasmon resonance (SPR) experiments were carried out on a Biacore 3000 SPR biosensor (Biacore InternationalAB). ..

Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis
Article Snippet: Neither mutation significantly affected binding to actin compared to wild-type protein ( ). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 2: caption a7 (A) Coomassie blue stained gel showing equivalent amounts (1.5 μg) of control GST, wild-type GST-P/A-C1-M, mutant GST-P/A-C1-M L259P, and mutant GST-P/A-C1-M L263R proteins used in the overlay and Biacore assays. .. Full length GST-P/A-C1-M recombinant proteins (~58 kDa) are denoted with an arrow; the preparations of both mutant proteins contain a very closely migrating degradation product (56–57 kDa), while a degradation product of ~50 kDa is present in all three protein preparations; non-continuous lanes are separated by a white line. (B) Real time kinetics evaluation of the interaction between wild-type or mutant GST-P/A-C1-M proteins and HMM using a Biacore 3000 SPR biosensor. (C) Kinetic measurements at equilibrium indicated that GST-P/A-C1-M L263R binding to HMM was decreased by ~5.5-fold compared to wild-type levels. (D) Equivalent amounts (3 μg) of purified actin were separated by SDS-PAGE, transferred to nitrocellulose membrane, and overlaid with 0.5 μg/mL of control GST-protein, wild-type GST-P/A-C1-M, or mutant GST-P/A-C1-M carrying the L259P or L263R mutation. ..

Article Title: A Systematic Investigation of Structure/Function Requirements for the Apolipoprotein A-I/Lecithin Cholesterol Acyltransferase Interaction Loop of High-density Lipoprotein
Article Snippet: .. Measurements of apparent Kd between hLCAT and rHDL were performed using a BIAcore 3000 SPR biosensor (BIAcore, AB, Uppsala, Sweden) following the methods of Jin et al (33) with modification. .. Briefly, approximately 8000 relative units (RU) of polyclonal antibody against apoA-I (Biodesign, Saco, ME) was immobilized on a CM5 sensor chip through primary amino groups using reactive esters as per manufacturer’s directions. rHDL was captured on the sensor chip through interaction with antibody against apoA-I by injecting 7 μM of rHDL at a flow rate of 15 μl/min in 10 mM PBS buffer (pH 7.4) into the flow cell.

Article Title: A Systematic Investigation of Structure/Function Requirements for the Apolipoprotein A-I/Lecithin Cholesterol Acyltransferase Interaction Loop of High-density Lipoprotein
Article Snippet: .. Measurements of apparent K d between hLCAT and rHDL were performed using a BIAcore 3000 SPR biosensor (BIAcore, AB, Uppsala, Sweden) following the methods of Jin et al. ( 33 ) with modification. .. Briefly, ∼8000 relative units of polyclonal antibody against apoA-I (Biodesign, Saco, ME) was immobilized on a CM5 sensor chip through primary amino groups using reactive esters as per the manufacturer's directions. rHDL was captured on the sensor chip through interaction with antibody against apoA-I by injecting 7 μ m rHDL at a flow rate of 15 μl/min in 10 m m PBS buffer (pH 7.4) into the flow cell.

Conjugation Assay:

Article Title: Open-sandwich molecular imprinting: making a recognition matrix with antigen-imprinted antibody fragments.
Article Snippet: A novel antibody−polymer conjugation method termed open-sandwich molecular imprinting (OS-MIP) has been proposed to produce a specific recognition matrix in the presence of a target antigen.. The resultant carboxymethyldextran matrix conjugated with two separate antibody variable region fragments imprinted with the cognate antigen showed higher antigen-binding capacity than non-imprinted ones and was successfully used to sensitively monitor multiple antigen binding/desorption events by a surface plasmon resonance biosensor.. Furthermore, when each fragment was labeled with different fluorophores before conjugation, the fluorescence signals of the matrix made by OS-MIP clearly showed an antigen concentration dependent increase in Förster resonance energy transfer between the two dyes.

Binding Assay:

Article Title: Open-sandwich molecular imprinting: making a recognition matrix with antigen-imprinted antibody fragments.
Article Snippet: A novel antibody−polymer conjugation method termed open-sandwich molecular imprinting (OS-MIP) has been proposed to produce a specific recognition matrix in the presence of a target antigen.. The resultant carboxymethyldextran matrix conjugated with two separate antibody variable region fragments imprinted with the cognate antigen showed higher antigen-binding capacity than non-imprinted ones and was successfully used to sensitively monitor multiple antigen binding/desorption events by a surface plasmon resonance biosensor.. Furthermore, when each fragment was labeled with different fluorophores before conjugation, the fluorescence signals of the matrix made by OS-MIP clearly showed an antigen concentration dependent increase in Förster resonance energy transfer between the two dyes.

Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis
Article Snippet: Neither mutation significantly affected binding to actin compared to wild-type protein ( ). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 2: caption a7 (A) Coomassie blue stained gel showing equivalent amounts (1.5 μg) of control GST, wild-type GST-P/A-C1-M, mutant GST-P/A-C1-M L259P, and mutant GST-P/A-C1-M L263R proteins used in the overlay and Biacore assays. .. Full length GST-P/A-C1-M recombinant proteins (~58 kDa) are denoted with an arrow; the preparations of both mutant proteins contain a very closely migrating degradation product (56–57 kDa), while a degradation product of ~50 kDa is present in all three protein preparations; non-continuous lanes are separated by a white line. (B) Real time kinetics evaluation of the interaction between wild-type or mutant GST-P/A-C1-M proteins and HMM using a Biacore 3000 SPR biosensor. (C) Kinetic measurements at equilibrium indicated that GST-P/A-C1-M L263R binding to HMM was decreased by ~5.5-fold compared to wild-type levels. (D) Equivalent amounts (3 μg) of purified actin were separated by SDS-PAGE, transferred to nitrocellulose membrane, and overlaid with 0.5 μg/mL of control GST-protein, wild-type GST-P/A-C1-M, or mutant GST-P/A-C1-M carrying the L259P or L263R mutation. ..

Recombinant:

Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis
Article Snippet: Neither mutation significantly affected binding to actin compared to wild-type protein ( ). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 2: caption a7 (A) Coomassie blue stained gel showing equivalent amounts (1.5 μg) of control GST, wild-type GST-P/A-C1-M, mutant GST-P/A-C1-M L259P, and mutant GST-P/A-C1-M L263R proteins used in the overlay and Biacore assays. .. Full length GST-P/A-C1-M recombinant proteins (~58 kDa) are denoted with an arrow; the preparations of both mutant proteins contain a very closely migrating degradation product (56–57 kDa), while a degradation product of ~50 kDa is present in all three protein preparations; non-continuous lanes are separated by a white line. (B) Real time kinetics evaluation of the interaction between wild-type or mutant GST-P/A-C1-M proteins and HMM using a Biacore 3000 SPR biosensor. (C) Kinetic measurements at equilibrium indicated that GST-P/A-C1-M L263R binding to HMM was decreased by ~5.5-fold compared to wild-type levels. (D) Equivalent amounts (3 μg) of purified actin were separated by SDS-PAGE, transferred to nitrocellulose membrane, and overlaid with 0.5 μg/mL of control GST-protein, wild-type GST-P/A-C1-M, or mutant GST-P/A-C1-M carrying the L259P or L263R mutation. ..

Mutagenesis:

Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis
Article Snippet: Neither mutation significantly affected binding to actin compared to wild-type protein ( ). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 2: caption a7 (A) Coomassie blue stained gel showing equivalent amounts (1.5 μg) of control GST, wild-type GST-P/A-C1-M, mutant GST-P/A-C1-M L259P, and mutant GST-P/A-C1-M L263R proteins used in the overlay and Biacore assays. .. Full length GST-P/A-C1-M recombinant proteins (~58 kDa) are denoted with an arrow; the preparations of both mutant proteins contain a very closely migrating degradation product (56–57 kDa), while a degradation product of ~50 kDa is present in all three protein preparations; non-continuous lanes are separated by a white line. (B) Real time kinetics evaluation of the interaction between wild-type or mutant GST-P/A-C1-M proteins and HMM using a Biacore 3000 SPR biosensor. (C) Kinetic measurements at equilibrium indicated that GST-P/A-C1-M L263R binding to HMM was decreased by ~5.5-fold compared to wild-type levels. (D) Equivalent amounts (3 μg) of purified actin were separated by SDS-PAGE, transferred to nitrocellulose membrane, and overlaid with 0.5 μg/mL of control GST-protein, wild-type GST-P/A-C1-M, or mutant GST-P/A-C1-M carrying the L259P or L263R mutation. ..

Purification:

Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis
Article Snippet: Neither mutation significantly affected binding to actin compared to wild-type protein ( ). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 2: caption a7 (A) Coomassie blue stained gel showing equivalent amounts (1.5 μg) of control GST, wild-type GST-P/A-C1-M, mutant GST-P/A-C1-M L259P, and mutant GST-P/A-C1-M L263R proteins used in the overlay and Biacore assays. .. Full length GST-P/A-C1-M recombinant proteins (~58 kDa) are denoted with an arrow; the preparations of both mutant proteins contain a very closely migrating degradation product (56–57 kDa), while a degradation product of ~50 kDa is present in all three protein preparations; non-continuous lanes are separated by a white line. (B) Real time kinetics evaluation of the interaction between wild-type or mutant GST-P/A-C1-M proteins and HMM using a Biacore 3000 SPR biosensor. (C) Kinetic measurements at equilibrium indicated that GST-P/A-C1-M L263R binding to HMM was decreased by ~5.5-fold compared to wild-type levels. (D) Equivalent amounts (3 μg) of purified actin were separated by SDS-PAGE, transferred to nitrocellulose membrane, and overlaid with 0.5 μg/mL of control GST-protein, wild-type GST-P/A-C1-M, or mutant GST-P/A-C1-M carrying the L259P or L263R mutation. ..

Membrane:

Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis
Article Snippet: Neither mutation significantly affected binding to actin compared to wild-type protein ( ). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 2: caption a7 (A) Coomassie blue stained gel showing equivalent amounts (1.5 μg) of control GST, wild-type GST-P/A-C1-M, mutant GST-P/A-C1-M L259P, and mutant GST-P/A-C1-M L263R proteins used in the overlay and Biacore assays. .. Full length GST-P/A-C1-M recombinant proteins (~58 kDa) are denoted with an arrow; the preparations of both mutant proteins contain a very closely migrating degradation product (56–57 kDa), while a degradation product of ~50 kDa is present in all three protein preparations; non-continuous lanes are separated by a white line. (B) Real time kinetics evaluation of the interaction between wild-type or mutant GST-P/A-C1-M proteins and HMM using a Biacore 3000 SPR biosensor. (C) Kinetic measurements at equilibrium indicated that GST-P/A-C1-M L263R binding to HMM was decreased by ~5.5-fold compared to wild-type levels. (D) Equivalent amounts (3 μg) of purified actin were separated by SDS-PAGE, transferred to nitrocellulose membrane, and overlaid with 0.5 μg/mL of control GST-protein, wild-type GST-P/A-C1-M, or mutant GST-P/A-C1-M carrying the L259P or L263R mutation. ..

Control:

Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis
Article Snippet: Neither mutation significantly affected binding to actin compared to wild-type protein ( ). fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 2: caption a7 (A) Coomassie blue stained gel showing equivalent amounts (1.5 μg) of control GST, wild-type GST-P/A-C1-M, mutant GST-P/A-C1-M L259P, and mutant GST-P/A-C1-M L263R proteins used in the overlay and Biacore assays. .. Full length GST-P/A-C1-M recombinant proteins (~58 kDa) are denoted with an arrow; the preparations of both mutant proteins contain a very closely migrating degradation product (56–57 kDa), while a degradation product of ~50 kDa is present in all three protein preparations; non-continuous lanes are separated by a white line. (B) Real time kinetics evaluation of the interaction between wild-type or mutant GST-P/A-C1-M proteins and HMM using a Biacore 3000 SPR biosensor. (C) Kinetic measurements at equilibrium indicated that GST-P/A-C1-M L263R binding to HMM was decreased by ~5.5-fold compared to wild-type levels. (D) Equivalent amounts (3 μg) of purified actin were separated by SDS-PAGE, transferred to nitrocellulose membrane, and overlaid with 0.5 μg/mL of control GST-protein, wild-type GST-P/A-C1-M, or mutant GST-P/A-C1-M carrying the L259P or L263R mutation. ..

Modification:

Article Title: A Systematic Investigation of Structure/Function Requirements for the Apolipoprotein A-I/Lecithin Cholesterol Acyltransferase Interaction Loop of High-density Lipoprotein
Article Snippet: .. Measurements of apparent Kd between hLCAT and rHDL were performed using a BIAcore 3000 SPR biosensor (BIAcore, AB, Uppsala, Sweden) following the methods of Jin et al (33) with modification. .. Briefly, approximately 8000 relative units (RU) of polyclonal antibody against apoA-I (Biodesign, Saco, ME) was immobilized on a CM5 sensor chip through primary amino groups using reactive esters as per manufacturer’s directions. rHDL was captured on the sensor chip through interaction with antibody against apoA-I by injecting 7 μM of rHDL at a flow rate of 15 μl/min in 10 mM PBS buffer (pH 7.4) into the flow cell.

Article Title: A Systematic Investigation of Structure/Function Requirements for the Apolipoprotein A-I/Lecithin Cholesterol Acyltransferase Interaction Loop of High-density Lipoprotein
Article Snippet: .. Measurements of apparent K d between hLCAT and rHDL were performed using a BIAcore 3000 SPR biosensor (BIAcore, AB, Uppsala, Sweden) following the methods of Jin et al. ( 33 ) with modification. .. Briefly, ∼8000 relative units of polyclonal antibody against apoA-I (Biodesign, Saco, ME) was immobilized on a CM5 sensor chip through primary amino groups using reactive esters as per the manufacturer's directions. rHDL was captured on the sensor chip through interaction with antibody against apoA-I by injecting 7 μ m rHDL at a flow rate of 15 μl/min in 10 m m PBS buffer (pH 7.4) into the flow cell.



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