Review





Similar Products

streptactin strep tag affinity purification procedure  (IBA Lifesciences)
96
IBA Lifesciences streptactin strep tag affinity purification procedure
Streptactin Strep Tag Affinity Purification Procedure, supplied by IBA Lifesciences, 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/affinity+purification+method/pmc10516654-253-7-16?v=IBA+Lifesciences
Average 96 stars, based on 1 article reviews
streptactin strep tag affinity purification procedure - by Bioz Stars, 2026-07
96/100 stars
  Buy from Supplier
high affinity purification method  (Bio Basic Canada)
86
Bio Basic Canada high affinity purification method
High Affinity Purification Method, supplied by Bio Basic Canada, 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/affinity+purification+method/pmc13044335-98-15-18?v=Bio+Basic+Canada
Average 86 stars, based on 1 article reviews
high affinity purification method - by Bioz Stars, 2026-07
86/100 stars
  Buy from Supplier
high affinity purification (hap) purification method  (Sangon Biotech)
90
Sangon Biotech high affinity purification (hap) purification method
High Affinity Purification (Hap) Purification Method, supplied by Sangon Biotech, 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/affinity+purification+method/pmc11754104__41551_2024_1278_MOESM1_ESM-31-20-26?v=Sangon+Biotech
Average 90 stars, based on 1 article reviews
high affinity purification (hap) purification method - by Bioz Stars, 2026-07
90/100 stars
  Buy from Supplier
ni-nta affinity-purification imac methods  (Qiagen)
90
Qiagen ni-nta affinity-purification imac methods
Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
Ni Nta Affinity Purification Imac Methods, supplied by Qiagen, 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/affinity+purification+method/pmc08063757-251-4-9?v=Qiagen
Average 90 stars, based on 1 article reviews
ni-nta affinity-purification imac methods - by Bioz Stars, 2026-07
90/100 stars
  Buy from Supplier
galectin-3 affinity purification method  (Galectin Therapeutics)
90
Galectin Therapeutics galectin-3 affinity purification method
Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
Galectin 3 Affinity Purification Method, supplied by Galectin Therapeutics, 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/affinity+purification+method/pmc07421905-137-12-12?v=Galectin+Therapeutics
Average 90 stars, based on 1 article reviews
galectin-3 affinity purification method - by Bioz Stars, 2026-07
90/100 stars
  Buy from Supplier
affinity purification method genscript igy  (GenScript corporation)
90
GenScript corporation affinity purification method genscript igy
Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
Affinity Purification Method Genscript Igy, supplied by GenScript corporation, 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/affinity+purification+method/pm31332484-149-6-11?v=GenScript+corporation
Average 90 stars, based on 1 article reviews
affinity purification method genscript igy - by Bioz Stars, 2026-07
90/100 stars
  Buy from Supplier
affinity purification method ligatrap igy  (LigaTrap Technologies)
90
LigaTrap Technologies affinity purification method ligatrap igy
Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
Affinity Purification Method Ligatrap Igy, supplied by LigaTrap Technologies, 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/affinity+purification+method/pm31332484-149-8-9?v=LigaTrap+Technologies
Average 90 stars, based on 1 article reviews
affinity purification method ligatrap igy - by Bioz Stars, 2026-07
90/100 stars
  Buy from Supplier
column affinity based method  (MACHEREY NAGEL)
96
MACHEREY NAGEL column affinity based method
Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
Column Affinity Based Method, supplied by MACHEREY NAGEL, 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/affinity+purification+method/pm29446652-65-9-15?v=MACHEREY+NAGEL
Average 96 stars, based on 1 article reviews
column affinity based method - by Bioz Stars, 2026-07
96/100 stars
  Buy from Supplier
protein g affinity purification method amicon proaffinity concentration kit  (Millipore)
90
Millipore protein g affinity purification method amicon proaffinity concentration kit
Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the <t>Ni-NTA-derivatized</t> sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.
Protein G Affinity Purification Method Amicon Proaffinity Concentration Kit, supplied by Millipore, 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/affinity+purification+method/10__1097_slash_tp__0000000000002516-34-22-19?v=Millipore
Average 90 stars, based on 1 article reviews
protein g affinity purification method amicon proaffinity concentration kit - by Bioz Stars, 2026-07
90/100 stars
  Buy from Supplier

Image Search Results


Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the Ni-NTA-derivatized sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.

Journal: The Journal of Biological Chemistry

Article Title: The DNA-binding protein HU is a molecular glue that attaches bacteria to extracellular DNA in biofilms

doi: 10.1016/j.jbc.2021.100532

Figure Lengend Snippet: Binding of HU to f-LPS. A , microscale thermophoresis (MST) dose–response curve for the binding of f-LPS by HU-A, based on varying concentrations of f-LPS and a fixed concentration of fluorescent tag-RFP–HU-A and plotting rates of reduction in fluorescence from tag-RFP–HU-A due to (temperature jump dependent) diffusion of molecules away from a microscopic volume of the solution being monitored inside a capillary, with different capillaries used for different f-LPS concentrations. B , raw microscale thermophoresis data traces for 16 capillaries containing different concentrations of f-LPS; blue and red bars indicate the beginning and ending of the time period used to calculate normalized rates of reduction in tag-RFP–HU-A fluorescence for capillaries over a 30-seconds-long laser-induced temperature jump; each curve plots the fall in fluorescence in a separate capillary, and the subsequent rise, over 5 s, after heating is switched off. C , biolayer interferometry (BLI) sensorgram showing the washing baseline (segment 1), binding of HU-B to the Ni-NTA-derivatized sensor (segment 2), washing baseline (segment 3), binding of f-LPS to HU-B (segment 4), and washing-based dissociation (segment 5). D , difference absorption spectroscopy (DAS) data monitoring binding of HU-B to f-LPS after zeroing of baseline; premixing spectra ( black ) and postmixing spectra ( red ) are used to detect hyperchromic/hypochromic effects in HU-B phenylalanine (∼265 nm) and RFP chromophore (550 nm) absorption bands due to binding. E–G , dynamic light scattering (DLS) monitoring changes in the size of 0.02-μm–filtered HU-B, f-LPS, and HU-B + f-LPS to detect noncovalent crosslinking of f-LPS by HU-B. H , denaturing SDS-PAGE investigating covalent (glutaraldehyde-mediated) crosslinking of HU-B by f-LPS. f-HU, free HU; f-LPS, free LPS; HU, highly abundant nucleoid-associated histone-like protein; LPS, lipopolysaccharide; RFP, red fluorescent protein.

Article Snippet: Proteins were purified using standard Ni-NTA affinity-purification IMAC methods (Qiagen QIAexpressionist) under nondenaturing conditions.

Techniques: Binding Assay, Microscale Thermophoresis, Concentration Assay, Fluorescence, Diffusion-based Assay, Spectroscopy, SDS Page