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3000 surface plasmon resonance (spr) biosensor  (Biacore)

 
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    Biacore 3000 surface plasmon resonance (spr) biosensor
    (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 <t>3000</t> <t>SPR</t> 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. Nitrocellulose membranes (Ponceau stain) and films (Western blots probed with GST-ab) were cropped to only include the area of expected signal. Densitometric quantification of at least three independent overlay/immunoblotting experiments indicated that neither mutation significantly affected binding to actin. Control GST-proteins did not bind actin.
    3000 Surface Plasmon Resonance (Spr) Biosensor, supplied by Biacore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/3000+surface+plasmon+resonance+(spr)+biosensor/3000++surface+plasmon+resonance+spr+system/pmc06688907-197-11-10
    Average 90 stars, based on 1 article reviews
    3000 surface plasmon resonance (spr) biosensor - by Bioz Stars, 2026-10
    90/100 stars

    Images

    1) Product Images from "Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis"

    Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis

    Journal: Human mutation

    doi: 10.1002/humu.23760

    (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. Nitrocellulose membranes (Ponceau stain) and films (Western blots probed with GST-ab) were cropped to only include the area of expected signal. Densitometric quantification of at least three independent overlay/immunoblotting experiments indicated that neither mutation significantly affected binding to actin. Control GST-proteins did not bind actin.
    Figure Legend Snippet: (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. Nitrocellulose membranes (Ponceau stain) and films (Western blots probed with GST-ab) were cropped to only include the area of expected signal. Densitometric quantification of at least three independent overlay/immunoblotting experiments indicated that neither mutation significantly affected binding to actin. Control GST-proteins did not bind actin.

    Techniques Used: Staining, Control, Mutagenesis, Recombinant, Binding Assay, Purification, SDS Page, Membrane, Western Blot

    Related Articles

    other:

    Article Title: T cell receptors
    Article Snippet: Protein concentration was determined using a Coomassie-binding assay (PerBio) and aliquots of biotinylated pHLA-A*02 molecules were stored frozen at −20° C. The BIAcore® 3000 surface plasmon resonance (SPR) biosensor measures changes in refractive index expressed in response units (RU) near a sensor surface within a small flow cell, a principle that can be used to detect receptor ligand interactions and to analyse their affinity and kinetic parameters.

    Article Title: A large-scale comparative analysis of affinity, thermodynamics and functional characteristics of interactions of twelve cytochrome P450 isoforms and their redox partners.
    Article Snippet: The aim of the present work was to establish the thermodynamic and functional differences in the protein-protein interactions between the components of the P450-dependent mitochondrial (mit) and microsomal (mic) monooxygenase systems using 12 different isoforms of cytochromes P450 and two redox partners, NADPH-dependent cytochrome P450 reductase (CPR) and adrenodoxin (Adx).. Comparative analysis of the affinity, thermodynamics, enzymatic activity and the ability for one-electron reduction has been carried out.. The study of protein-protein interactions to determine the equilibrium dissociation constants (Kd) was performed using surface plasmon resonance (SPR) biosensor Biacore 3000.

    Article Title: A Tetravalent Bispecific Antibody Selectively Inhibits Diverse FGFR3 Oncogenic Variants
    Article Snippet: Human, monkey, murine FGFR3b or human FGFR3c ECD binding to purified anti-FGFR3 antibodies were determined using a real-time surface plasmon resonance biosensor technology (Biacore 3000 or Biacore 4000).

    Article Title: Human antibodies to GFRα3 and methods of making thereof
    Article Snippet: Binding associative and dissociative rate constants (ka and kd, respectively) and calculated equilibrium dissociation constants and dissociative half-lives (KD and t1/2, respectively) for antigen binding to anti-mouse GFRα3 antibodies were determined using a real-time surface plasmon resonance biosensor (Biacore 3000) assay at 25° C. Antibodies were tested for binding to mouse GFRα3 expressed with myc-myc-hexahistidine tag (mGFRα3-MMH; SEQ ID: 379).

    Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis
    Article Snippet: These were subsequently used in real-time kinetic analysis using a Biacore 3000 surface plasmon resonance (SPR) biosensor to monitor their binding affinity, K D , to heavy meromyosin (HMM; – ).

    SPR Assay:

    Article Title: Supporting Information Experimental Procedures
    Article Snippet: .. Kinetics analysis of DcR3-TL1A interaction by Surface Plasmon Resonance All experiments were performed with a Surface Plasmon Resonance-based biosensor instrument Biacore 3000 (Biacore) at 25 oC. .. The recombinant human DcR3-Ig fusion protein (R&D Systems, Minneapolis, MN) was immobilized on CM5 sensor chips by random free amine coupling according to the manufacturer’s recommendation.

    Article Title: Discovery of a Novel Chemotype of Histone Lysine Methyltransferase EHMT1/2 (GLP/G9a) Inhibitors: Rational Design, Synthesis, Biological Evaluation, and Co-crystal Structure
    Article Snippet: Each compound was tested in duplicate samples and data analysed using MO Affinity Analysis software (NanoTemper Technologies). .. Surface Plasmon Resonance SPR analyses were performed on a Biacore 3000 optical biosensor equipped with research-grade CM5 sensor chips (Biacore AB). ..



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    (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 <t>3000</t> <t>SPR</t> 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. Nitrocellulose membranes (Ponceau stain) and films (Western blots probed with GST-ab) were cropped to only include the area of expected signal. Densitometric quantification of at least three independent overlay/immunoblotting experiments indicated that neither mutation significantly affected binding to actin. Control GST-proteins did not bind actin.
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    Image Search Results


    (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. Nitrocellulose membranes (Ponceau stain) and films (Western blots probed with GST-ab) were cropped to only include the area of expected signal. Densitometric quantification of at least three independent overlay/immunoblotting experiments indicated that neither mutation significantly affected binding to actin. Control GST-proteins did not bind actin.

    Journal: Human mutation

    Article Title: Heterozygous Variants in MYBPC1 are Associated with an Expanded Neuromuscular Phenotype beyond Arthrogryposis

    doi: 10.1002/humu.23760

    Figure Lengend Snippet: (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. Nitrocellulose membranes (Ponceau stain) and films (Western blots probed with GST-ab) were cropped to only include the area of expected signal. Densitometric quantification of at least three independent overlay/immunoblotting experiments indicated that neither mutation significantly affected binding to actin. Control GST-proteins did not bind actin.

    Article Snippet: These were subsequently used in real-time kinetic analysis using a Biacore 3000 surface plasmon resonance (SPR) biosensor to monitor their binding affinity, K D , to heavy meromyosin (HMM; – ).

    Techniques: Staining, Control, Mutagenesis, Recombinant, Binding Assay, Purification, SDS Page, Membrane, Western Blot