spr spectroscopy-based binding analysis Search Results


human fcrγiiia cd16a receptor  (R&D Systems)
94
R&D Systems human fcrγiiia cd16a receptor
Structural and functional characterization platform used for assessing similarity of Rituximab biosimilars vs. Ristova®.
Human Fcrγiiia Cd16a Receptor, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/spr+spectroscopy-based+binding+analysis/pmc05800382-476-9-13?v=R%26D+Systems
Average 94 stars, based on 1 article reviews
human fcrγiiia cd16a receptor - by Bioz Stars, 2026-08
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pfhsp90  (StressMarq)
90
StressMarq pfhsp90
(A) Illustration of geldanamycin (GA, left) and PU-H71 (right) docked within the ATP-binding site of <t>PfHsp90.</t> The models were generated using the PfHsp90 crystal structure (PDB ID: 3K60) . By convention, the electrostatic potential surface in the background denotes acidic residues in red and basic residues in blue. (B) Surface plasmon resonance (SPR) measurements for PU-H71 binding to the ATP-binding domain of PfHsp90. The colors on the sensorgrams represent varying concentrations of the respective drug (5–1000 µM) injected over the surface with the immobilized PfHsp90. The steady state responses were fitted using non-linear regression to a single binding site model (as shown on the right) to obtain the K d value indicated. The number in parentheses represents standard error on the K d obtained from fits. The sensorgrams shown have been double referenced as described previously . (C) 17-AAG was used as a positive control drug. (D) SPR measurements for PU-H71 binding of the R98K mutant ATP-binding domain of PfHsp90. (E) Full-length PfHsp90 was expressed and ATPase activity tested in the presence of PU-H71. Results are shown as a percentage of total ATPase activity in the absence of drug and IC 50 indicated (511 nM) for a single experiment. Positive control drug treatments included radicicol (144 nM) and 17-AAG (146 nM). The inset shows the logarithmic curve fitting of ATPase activity with increasing concentration of PU-H71.
Pfhsp90, supplied by StressMarq, 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/spr+spectroscopy-based+binding+analysis/pmc03787104-205-34-35?v=StressMarq
Average 90 stars, based on 1 article reviews
pfhsp90 - by Bioz Stars, 2026-08
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dna sequences  (Thermo Fisher)
99
Thermo Fisher dna sequences
(A) Illustration of geldanamycin (GA, left) and PU-H71 (right) docked within the ATP-binding site of <t>PfHsp90.</t> The models were generated using the PfHsp90 crystal structure (PDB ID: 3K60) . By convention, the electrostatic potential surface in the background denotes acidic residues in red and basic residues in blue. (B) Surface plasmon resonance (SPR) measurements for PU-H71 binding to the ATP-binding domain of PfHsp90. The colors on the sensorgrams represent varying concentrations of the respective drug (5–1000 µM) injected over the surface with the immobilized PfHsp90. The steady state responses were fitted using non-linear regression to a single binding site model (as shown on the right) to obtain the K d value indicated. The number in parentheses represents standard error on the K d obtained from fits. The sensorgrams shown have been double referenced as described previously . (C) 17-AAG was used as a positive control drug. (D) SPR measurements for PU-H71 binding of the R98K mutant ATP-binding domain of PfHsp90. (E) Full-length PfHsp90 was expressed and ATPase activity tested in the presence of PU-H71. Results are shown as a percentage of total ATPase activity in the absence of drug and IC 50 indicated (511 nM) for a single experiment. Positive control drug treatments included radicicol (144 nM) and 17-AAG (146 nM). The inset shows the logarithmic curve fitting of ATPase activity with increasing concentration of PU-H71.
Dna Sequences, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/spr+spectroscopy-based+binding+analysis/us11432547-285-8-31?v=Thermo+Fisher
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dna sequences - by Bioz Stars, 2026-08
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surfactant p20  (Cytiva Europe)
96
Cytiva Europe surfactant p20
(A) Illustration of geldanamycin (GA, left) and PU-H71 (right) docked within the ATP-binding site of <t>PfHsp90.</t> The models were generated using the PfHsp90 crystal structure (PDB ID: 3K60) . By convention, the electrostatic potential surface in the background denotes acidic residues in red and basic residues in blue. (B) Surface plasmon resonance (SPR) measurements for PU-H71 binding to the ATP-binding domain of PfHsp90. The colors on the sensorgrams represent varying concentrations of the respective drug (5–1000 µM) injected over the surface with the immobilized PfHsp90. The steady state responses were fitted using non-linear regression to a single binding site model (as shown on the right) to obtain the K d value indicated. The number in parentheses represents standard error on the K d obtained from fits. The sensorgrams shown have been double referenced as described previously . (C) 17-AAG was used as a positive control drug. (D) SPR measurements for PU-H71 binding of the R98K mutant ATP-binding domain of PfHsp90. (E) Full-length PfHsp90 was expressed and ATPase activity tested in the presence of PU-H71. Results are shown as a percentage of total ATPase activity in the absence of drug and IC 50 indicated (511 nM) for a single experiment. Positive control drug treatments included radicicol (144 nM) and 17-AAG (146 nM). The inset shows the logarithmic curve fitting of ATPase activity with increasing concentration of PU-H71.
Surfactant P20, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/spr+spectroscopy-based+binding+analysis/custom%40br100054%4025126676?v=Cytiva+Europe
Average 96 stars, based on 1 article reviews
surfactant p20 - by Bioz Stars, 2026-08
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Image Search Results


Structural and functional characterization platform used for assessing similarity of Rituximab biosimilars vs. Ristova®.

Journal: mAbs

Article Title: Assessment of structural and functional similarity of biosimilar products: Rituximab as a case study

doi: 10.1080/19420862.2017.1402996

Figure Lengend Snippet: Structural and functional characterization platform used for assessing similarity of Rituximab biosimilars vs. Ristova®.

Article Snippet: Surface plasmon resonance The kinetics of rituximab binding to human FcRγIIIa (CD16a) receptor (R&D systems; Cat# 4325-FC) was determined by Biacore X100TM (GE Healthcare).

Techniques: Functional Assay, Bioprocessing, Sequencing, Circular Dichroism, Spectroscopy, Fluorescence, Migration, Activity Assay, Binding Assay, Cell Based Assay

(A) Illustration of geldanamycin (GA, left) and PU-H71 (right) docked within the ATP-binding site of PfHsp90. The models were generated using the PfHsp90 crystal structure (PDB ID: 3K60) . By convention, the electrostatic potential surface in the background denotes acidic residues in red and basic residues in blue. (B) Surface plasmon resonance (SPR) measurements for PU-H71 binding to the ATP-binding domain of PfHsp90. The colors on the sensorgrams represent varying concentrations of the respective drug (5–1000 µM) injected over the surface with the immobilized PfHsp90. The steady state responses were fitted using non-linear regression to a single binding site model (as shown on the right) to obtain the K d value indicated. The number in parentheses represents standard error on the K d obtained from fits. The sensorgrams shown have been double referenced as described previously . (C) 17-AAG was used as a positive control drug. (D) SPR measurements for PU-H71 binding of the R98K mutant ATP-binding domain of PfHsp90. (E) Full-length PfHsp90 was expressed and ATPase activity tested in the presence of PU-H71. Results are shown as a percentage of total ATPase activity in the absence of drug and IC 50 indicated (511 nM) for a single experiment. Positive control drug treatments included radicicol (144 nM) and 17-AAG (146 nM). The inset shows the logarithmic curve fitting of ATPase activity with increasing concentration of PU-H71.

Journal: PLoS ONE

Article Title: A Purine Analog Synergizes with Chloroquine (CQ) by Targeting Plasmodium falciparum Hsp90 (PfHsp90)

doi: 10.1371/journal.pone.0075446

Figure Lengend Snippet: (A) Illustration of geldanamycin (GA, left) and PU-H71 (right) docked within the ATP-binding site of PfHsp90. The models were generated using the PfHsp90 crystal structure (PDB ID: 3K60) . By convention, the electrostatic potential surface in the background denotes acidic residues in red and basic residues in blue. (B) Surface plasmon resonance (SPR) measurements for PU-H71 binding to the ATP-binding domain of PfHsp90. The colors on the sensorgrams represent varying concentrations of the respective drug (5–1000 µM) injected over the surface with the immobilized PfHsp90. The steady state responses were fitted using non-linear regression to a single binding site model (as shown on the right) to obtain the K d value indicated. The number in parentheses represents standard error on the K d obtained from fits. The sensorgrams shown have been double referenced as described previously . (C) 17-AAG was used as a positive control drug. (D) SPR measurements for PU-H71 binding of the R98K mutant ATP-binding domain of PfHsp90. (E) Full-length PfHsp90 was expressed and ATPase activity tested in the presence of PU-H71. Results are shown as a percentage of total ATPase activity in the absence of drug and IC 50 indicated (511 nM) for a single experiment. Positive control drug treatments included radicicol (144 nM) and 17-AAG (146 nM). The inset shows the logarithmic curve fitting of ATPase activity with increasing concentration of PU-H71.

Article Snippet: To determine whether the mechanism of the synergism with CQ might be related to an interaction between PfCRT and the PfHsp90 complex, we performed co-immunoprecipitation of W2 parasite protein extracts with antibodies specific to PfHsp90 (StressMarq, rabbit polyclonal IgM) or PfCRT (MR4, polyclonal rabbit serum).

Techniques: Binding Assay, Generated, SPR Assay, Injection, Positive Control, Mutagenesis, Activity Assay, Concentration Assay

The Coomassie stained gels are shown to indicate loading. (A) Under non-denaturing conditions, immunoprecipitation with anti-PfHsp90 (upper panel) pulled down both itself and the PfCRT as demonstrated by western blot. The converse experiment (with anti-PfCRT immunoprecipitation (lower panel) achieved the reciprocal result. The mock control used was beads alone plus extracts. (B) Anti-PfCRT (top) and anti-PfHsp90 (middle) Western blots of immunoprecipitates under denaturing conditions with associated controls. These western blots are displayed as composites because they were run on two separate gels. The exposure levels were matched. The lowermost panel displays western blots of both PfHsp90 and PfCRT from P. falciparum culture protein extracts. (C) Anti-PfCRT Western blot of proteins which bound to histidine-tagged full length (FL) PfHsp90 coupled to Ni-NTA beads. (D) Extracts from P. falciparum strain W2 treated and untreated for 24 hours with 111 nM PU-H71 and immunoblotted with anti-PfCRT and anti-PfHsp90 antibody to determine the level of PfCRT and PfHsp90 available following PfHsp90 inhibition. The upper right panel demonstrates equal loading of protein in drug treated and untreated fractions. (E) Unweighted protein-protein interaction network of LC-MS/MS analyzed immunoprecipitates using anti-PfHsp90 and anti-PfCRT. The complete list of constituents in the interactome is available in . The image was generated using Cytoscape v2.8 . Lines connecting proteins suggest a direct interaction.

Journal: PLoS ONE

Article Title: A Purine Analog Synergizes with Chloroquine (CQ) by Targeting Plasmodium falciparum Hsp90 (PfHsp90)

doi: 10.1371/journal.pone.0075446

Figure Lengend Snippet: The Coomassie stained gels are shown to indicate loading. (A) Under non-denaturing conditions, immunoprecipitation with anti-PfHsp90 (upper panel) pulled down both itself and the PfCRT as demonstrated by western blot. The converse experiment (with anti-PfCRT immunoprecipitation (lower panel) achieved the reciprocal result. The mock control used was beads alone plus extracts. (B) Anti-PfCRT (top) and anti-PfHsp90 (middle) Western blots of immunoprecipitates under denaturing conditions with associated controls. These western blots are displayed as composites because they were run on two separate gels. The exposure levels were matched. The lowermost panel displays western blots of both PfHsp90 and PfCRT from P. falciparum culture protein extracts. (C) Anti-PfCRT Western blot of proteins which bound to histidine-tagged full length (FL) PfHsp90 coupled to Ni-NTA beads. (D) Extracts from P. falciparum strain W2 treated and untreated for 24 hours with 111 nM PU-H71 and immunoblotted with anti-PfCRT and anti-PfHsp90 antibody to determine the level of PfCRT and PfHsp90 available following PfHsp90 inhibition. The upper right panel demonstrates equal loading of protein in drug treated and untreated fractions. (E) Unweighted protein-protein interaction network of LC-MS/MS analyzed immunoprecipitates using anti-PfHsp90 and anti-PfCRT. The complete list of constituents in the interactome is available in . The image was generated using Cytoscape v2.8 . Lines connecting proteins suggest a direct interaction.

Article Snippet: To determine whether the mechanism of the synergism with CQ might be related to an interaction between PfCRT and the PfHsp90 complex, we performed co-immunoprecipitation of W2 parasite protein extracts with antibodies specific to PfHsp90 (StressMarq, rabbit polyclonal IgM) or PfCRT (MR4, polyclonal rabbit serum).

Techniques: Staining, Immunoprecipitation, Western Blot, Control, Inhibition, Liquid Chromatography with Mass Spectroscopy, Generated

(A) The Thr163Pro mutation is depicted computationally in the crystal structure of the PfHsp90 ATP-binding domain . (B) The presence of this mutation resulted in doubling of the PU-H71 IC 50 in the cell-based assay (a single representative experiment performed in duplicate is shown). (C) Synergy between PU-H71 and CQ in the Thr163Pro mutant was still observed based on sum FIC ratio ≤0.5. The inset provides a magnified view of the FIC 50 ratios for the different PU-H71 and CQ drug combinations in the mutant strain.

Journal: PLoS ONE

Article Title: A Purine Analog Synergizes with Chloroquine (CQ) by Targeting Plasmodium falciparum Hsp90 (PfHsp90)

doi: 10.1371/journal.pone.0075446

Figure Lengend Snippet: (A) The Thr163Pro mutation is depicted computationally in the crystal structure of the PfHsp90 ATP-binding domain . (B) The presence of this mutation resulted in doubling of the PU-H71 IC 50 in the cell-based assay (a single representative experiment performed in duplicate is shown). (C) Synergy between PU-H71 and CQ in the Thr163Pro mutant was still observed based on sum FIC ratio ≤0.5. The inset provides a magnified view of the FIC 50 ratios for the different PU-H71 and CQ drug combinations in the mutant strain.

Article Snippet: To determine whether the mechanism of the synergism with CQ might be related to an interaction between PfCRT and the PfHsp90 complex, we performed co-immunoprecipitation of W2 parasite protein extracts with antibodies specific to PfHsp90 (StressMarq, rabbit polyclonal IgM) or PfCRT (MR4, polyclonal rabbit serum).

Techniques: Mutagenesis, Binding Assay, Cell Based Assay