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Microarrays Inc applied (ami) array
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SCIENION sciflexarrayer s3 non contact microarray
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
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Aushon Biosystems 2470 microarrayer
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
2470 Microarrayer, supplied by Aushon Biosystems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Gesellschaft fur Silizium-Mikrosysteme nanoplotter 2.1
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
Nanoplotter 2.1, supplied by Gesellschaft fur Silizium-Mikrosysteme, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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CapitalBio Corporation contact-printing robotic smartarrayer 48 microarrayer
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
Contact Printing Robotic Smartarrayer 48 Microarrayer, supplied by CapitalBio Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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SCIENION non contact sciflexarrayer s12 microarray spotter
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
Non Contact Sciflexarrayer S12 Microarray Spotter, supplied by SCIENION, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Digilab Inc contact microarrayer omnigrid micro
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
Contact Microarrayer Omnigrid Micro, supplied by Digilab Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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M2-Automation 4/9 non-contact microarray
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
4/9 Non Contact Microarray, supplied by M2-Automation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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BioDot Inc non-contact microarrayer robot
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
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Gesellschaft fur Silizium-Mikrosysteme non-contact microarray
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
Non Contact Microarray, supplied by Gesellschaft fur Silizium-Mikrosysteme, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Engineering Arts LLC non-contact piezoelectric dispensing microarrayer
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
Non Contact Piezoelectric Dispensing Microarrayer, supplied by Engineering Arts LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Engineering Arts LLC non-contact piezoelectric dispensing microarrayer rainmaker-au302
Fig. 4 | Glycan <t>microarray</t> studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.
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Image Search Results


Fig. 4 | Glycan microarray studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.

Journal: Nature chemistry

Article Title: Synthetic O-acetylated sialosides facilitate functional receptor identification for human respiratory viruses.

doi: 10.1038/s41557-021-00655-9

Figure Lengend Snippet: Fig. 4 | Glycan microarray studies reveal binding patterns associated with host specificities. a, Column graphs of viral receptor selectivities. See Supplementary Fig. 9 for the chemical structures of the compounds. Additional results with different concentrations of proteins are presented in Supplementary Fig. 12. Columns show the background-subtracted average relative fluorescence unit (RFU) values of four replicates. Error bars indicate the s.d. of the RFUs. b, Heat-map presentations of viral receptor selectivities. In the heat map, the signal intensities are normalized with the highest value in each protein defined as 1.0 and shown with a colour gradient. Concentrations of Fc-tagged proteins presented are: BCoV S1A 0.3 μg ml–1, OC43 S1A 0.3 μg ml–1, HKU1 S1A 30 μg ml–1, ICV HEF 0.3 μg ml–1, IDV HEF 0.3 μg ml–1, porcine torovirus (PToV) HE 3 μg ml–1, BToV HE 3 μg ml–1, BCoV HE 3 μg ml–1, ECoV HE 3 μg ml–1, RbCoV HE 3 μg ml–1, CRCoV HE 3 μg ml–1, MHV-S HE 3 μg ml–1, ECoV S1A 3 μg ml–1, RbCoV S1A 3 μg ml–1 and CRCoV S1A 10 μg ml–1. Representative surface dissociation constants (Kd,surf) were obtained for the binding of HKU1 S1A with compounds 3g (9-O-Ac, 60 nM) and 3d (7,9-di-O-Ac, 85 nM). See supplementary Fig. 13 for binding curves. Sialoforms 1b and 2b (4,7-di-O-Ac Neu5Ac) were not included in the library because they have not been documented to be naturally occurring.

Article Snippet: The biotinylated compounds were printed on streptavidin-coated glass slides (SuperStreptavidin Microarray Substrate Slides, ArrayIt Inc) using a Scienion sciFLEXARRAYER S3 non-contact microarray equipped with a Scienion PDC80 nozzle (Scienion Inc).

Techniques: Glycoproteomics, Microarray, Binding Assay, Fluorescence