lactose Search Results


lacnac  (Biosynth Carbosynth)
92
Biosynth Carbosynth lacnac
Competitive inhibition of Gal-3 binding to ASF by glycopolymers 24 – 39 determined by ELISA
Lacnac, supplied by Biosynth Carbosynth, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lactose/pmc06146777-77-8-11?v=Biosynth+Carbosynth
Average 92 stars, based on 1 article reviews
lacnac - by Bioz Stars, 2026-08
92/100 stars
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d lactose  (Santa Cruz Biotechnology)
92
Santa Cruz Biotechnology d lactose
Competitive inhibition of Gal-3 binding to ASF by glycopolymers 24 – 39 determined by ELISA
D Lactose, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lactose/10__1128_slash_jvi__01045___17-193-16-17?v=Santa+Cruz+Biotechnology
Average 92 stars, based on 1 article reviews
d lactose - by Bioz Stars, 2026-08
92/100 stars
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galectin 1 antibody  (Proteintech)
93
Proteintech galectin 1 antibody
Competitive inhibition of Gal-3 binding to ASF by glycopolymers 24 – 39 determined by ELISA
Galectin 1 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lactose/pmc09638718-447-26-29?v=Proteintech
Average 93 stars, based on 1 article reviews
galectin 1 antibody - by Bioz Stars, 2026-08
93/100 stars
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rabbit polyclonal anti galectin 2  (Proteintech)
91
Proteintech rabbit polyclonal anti galectin 2
Competitive inhibition of Gal-3 binding to ASF by glycopolymers 24 – 39 determined by ELISA
Rabbit Polyclonal Anti Galectin 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lactose/pmc04951281-311-39-43?v=Proteintech
Average 91 stars, based on 1 article reviews
rabbit polyclonal anti galectin 2 - by Bioz Stars, 2026-08
91/100 stars
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human alpha lactalbumin  (Athens Research)
90
Athens Research human alpha lactalbumin
Native folds of <t>alpha</t> <t>lactalbumin</t> and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively
Human Alpha Lactalbumin, supplied by Athens Research, 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/lactose/pmc06318237-17-0-3?v=Athens+Research
Average 90 stars, based on 1 article reviews
human alpha lactalbumin - by Bioz Stars, 2026-08
90/100 stars
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d glucose 1 14c lactose  (Revvity)
91
Revvity d glucose 1 14c lactose
Native folds of <t>alpha</t> <t>lactalbumin</t> and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively
D Glucose 1 14c Lactose, supplied by Revvity, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lactose/10__1074_slash_jbc__m109__096305-56-31-32?v=Revvity
Average 91 stars, based on 1 article reviews
d glucose 1 14c lactose - by Bioz Stars, 2026-08
91/100 stars
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gal4 transcription factor  (ProSci Incorporated)
90
ProSci Incorporated gal4 transcription factor
Native folds of <t>alpha</t> <t>lactalbumin</t> and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively
Gal4 Transcription Factor, supplied by ProSci Incorporated, 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/lactose/pmc03372931-92-23-5?v=ProSci+Incorporated
Average 90 stars, based on 1 article reviews
gal4 transcription factor - by Bioz Stars, 2026-08
90/100 stars
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d lactose  (Thermo Fisher)
94
Thermo Fisher d lactose
Native folds of <t>alpha</t> <t>lactalbumin</t> and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively
D Lactose, supplied by Thermo Fisher, 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/lactose/10__3390_slash_sym13112053-46-16-21?v=Thermo+Fisher
Average 94 stars, based on 1 article reviews
d lactose - by Bioz Stars, 2026-08
94/100 stars
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lactose  (Biosynth Carbosynth)
93
Biosynth Carbosynth lactose
Native folds of <t>alpha</t> <t>lactalbumin</t> and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively
Lactose, supplied by Biosynth Carbosynth, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lactose/us09828599-363-0-4?v=Biosynth+Carbosynth
Average 93 stars, based on 1 article reviews
lactose - by Bioz Stars, 2026-08
93/100 stars
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violet red bile lactose agar vrbl  (Bio-Rad)
86
Bio-Rad violet red bile lactose agar vrbl
Native folds of <t>alpha</t> <t>lactalbumin</t> and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively
Violet Red Bile Lactose Agar Vrbl, supplied by Bio-Rad, 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/lactose/10__5897_slash_ajmr2016__8427-66-5-11?v=Bio-Rad
Average 86 stars, based on 1 article reviews
violet red bile lactose agar vrbl - by Bioz Stars, 2026-08
86/100 stars
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antibody sc 474  (Santa Cruz Biotechnology)
91
Santa Cruz Biotechnology antibody sc 474
Native folds of <t>alpha</t> <t>lactalbumin</t> and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively
Antibody Sc 474, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lactose/10__1128_slash_mcb__18__8__4537-99-11-14?v=Santa+Cruz+Biotechnology
Average 91 stars, based on 1 article reviews
antibody sc 474 - by Bioz Stars, 2026-08
91/100 stars
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ldh a lactose dehydrogenase a  (Santa Cruz Biotechnology)
94
Santa Cruz Biotechnology ldh a lactose dehydrogenase a
Native folds of <t>alpha</t> <t>lactalbumin</t> and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively
Ldh A Lactose Dehydrogenase A, supplied by Santa Cruz Biotechnology, 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/lactose/pmc09565115-15-0-10?v=Santa+Cruz+Biotechnology
Average 94 stars, based on 1 article reviews
ldh a lactose dehydrogenase a - by Bioz Stars, 2026-08
94/100 stars
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Image Search Results


Competitive inhibition of Gal-3 binding to ASF by glycopolymers 24 – 39 determined by ELISA

Journal: Journal of Nanobiotechnology

Article Title: Biocompatible glyconanomaterials based on HPMA-copolymer for specific targeting of galectin-3

doi: 10.1186/s12951-018-0399-1

Figure Lengend Snippet: Competitive inhibition of Gal-3 binding to ASF by glycopolymers 24 – 39 determined by ELISA

Article Snippet: Lactose (Galβ1,4Glc) was bought from Lachema (CZ) and LacNAc (Galβ1,4GlcNAc) from Carbosynth Ltd. (UK). p -Nitrophenyl 2-acetamido-2-deoxy-β- d -galactopyranoside ( p NP-GalNAc) and p -nitrophenyl 2-acetamido-2-deoxy-β- d -glucopyranoside ( p NP-GlcNAc) were obtained from Gold Biotechnology (MO, USA).

Techniques: Inhibition, Binding Assay, Glycoproteomics

Native folds of alpha lactalbumin and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively

Journal: Journal of the American Society for Mass Spectrometry

Article Title: Quantitative Evaluation of Native Protein Folds and Assemblies by Hydrogen Deuterium Exchange Mass Spectrometry (HDX-MS)

doi: 10.1007/s13361-018-2070-3

Figure Lengend Snippet: Native folds of alpha lactalbumin and barnase investigated by HDX-MS: ( a , e ) Mirror plots comparing experimental (positive) and simulated (negative) HDX-MS outputs. Experimental data were acquired at 0.25, 1, 5, 20, 60, 240 and 480 min at 293.15 K (coloured dark blue through red respectively). The pink bars denote the time-averaged difference in RFU between the experimental and simulated data and are shown to highlight areas of significant change. ( b , f ) Scatterplot comparing observed and simulated HDX-MS data of all RFU time points with different labelling times coloured as in ( a ). ( c , g ) The relationship between the RMSE and RMSD of 1000 decoys. The RMSE was calculated by pairwise comparison of the simulated and experimental HDX-MS data and the RMSD determined by alignment with the crystal structure. ( d – h ) ROC plots demonstrating the ability of the HDX-MS simulations to classify protein structures. Decoys with an RMSD ≤ 2.5 Å with the crystal structure were classified as native. Alpha lactalbumin and barnase data are shown in the upper and lower four figures, respectively

Article Snippet: Human alpha lactalbumin (Athens Research and Technology Inc., Athens, USA), enolase from baker’s yeast (Sigma-Aldrich Ltd., Dorset, UK) and serum amyloid P component (SAP) from human serum (Merck Chemicals Ltd., Nottingham, UK) were purchased as lyophilised powder, and barnase was prepared in-house.

Techniques: Comparison

peptide maps of alpha lactalbumin and barnase: The peptide maps of alpha lactalbumin (blue) and barnase (red) that comprise the HDX-MS data of these proteins are shown along with the respective number of peptides, coverage and redundancies. The ~ 20 residue region missing from the alpha lactalbumin data spans two of the four disulphide bonds of the protein

Journal: Journal of the American Society for Mass Spectrometry

Article Title: Quantitative Evaluation of Native Protein Folds and Assemblies by Hydrogen Deuterium Exchange Mass Spectrometry (HDX-MS)

doi: 10.1007/s13361-018-2070-3

Figure Lengend Snippet: peptide maps of alpha lactalbumin and barnase: The peptide maps of alpha lactalbumin (blue) and barnase (red) that comprise the HDX-MS data of these proteins are shown along with the respective number of peptides, coverage and redundancies. The ~ 20 residue region missing from the alpha lactalbumin data spans two of the four disulphide bonds of the protein

Article Snippet: Human alpha lactalbumin (Athens Research and Technology Inc., Athens, USA), enolase from baker’s yeast (Sigma-Aldrich Ltd., Dorset, UK) and serum amyloid P component (SAP) from human serum (Merck Chemicals Ltd., Nottingham, UK) were purchased as lyophilised powder, and barnase was prepared in-house.

Techniques: Residue