piezoelectric non-contact microarray robot sprint Search Results


nanoplotter 2.1  (Gesellschaft fur Silizium-Mikrosysteme)
90
Gesellschaft fur Silizium-Mikrosysteme nanoplotter 2.1
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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non-contact piezoelectric dispensing microarrayer  (Engineering Arts LLC)
90
Engineering Arts LLC non-contact piezoelectric dispensing microarrayer
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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non-contact piezoelectric dispensing microarrayer rainmaker-au302  (Engineering Arts LLC)
90
Engineering Arts LLC non-contact piezoelectric dispensing microarrayer rainmaker-au302
Non Contact Piezoelectric Dispensing Microarrayer Rainmaker Au302, 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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noncontact piezoelectric microarrayer nanoplotter 2.1e  (Gesellschaft fur Silizium-Mikrosysteme)
90
Gesellschaft fur Silizium-Mikrosysteme noncontact piezoelectric microarrayer nanoplotter 2.1e
Noncontact Piezoelectric Microarrayer Nanoplotter 2.1e, 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
https://www.bioz.com/result/noncontact piezoelectric microarrayer nanoplotter 2.1e/product/Gesellschaft fur Silizium-Mikrosysteme
Average 90 stars, based on 1 article reviews
noncontact piezoelectric microarrayer nanoplotter 2.1e - by Bioz Stars, 2026-06
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piezoelectric non-contact microarray dispenser (nano-plotter)  (Gesellschaft fur Silizium-Mikrosysteme)
90
Gesellschaft fur Silizium-Mikrosysteme piezoelectric non-contact microarray dispenser (nano-plotter)
Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen <t>microarray.</t> ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.
Piezoelectric Non Contact Microarray Dispenser (Nano Plotter), 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
https://www.bioz.com/result/piezoelectric non-contact microarray dispenser (nano-plotter)/product/Gesellschaft fur Silizium-Mikrosysteme
Average 90 stars, based on 1 article reviews
piezoelectric non-contact microarray dispenser (nano-plotter) - by Bioz Stars, 2026-06
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piezoelectric non contact printing  (SCIENION)
96
SCIENION piezoelectric non contact printing
Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen <t>microarray.</t> ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.
Piezoelectric Non Contact Printing, supplied by SCIENION, 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/result/piezoelectric non contact printing/product/SCIENION
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piezoelectric non contact printing - by Bioz Stars, 2026-06
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ultra-thin, nitrocellulose-coated microscope slides path slides  (GenTel BioSurfaces)
90
GenTel BioSurfaces ultra-thin, nitrocellulose-coated microscope slides path slides
Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen <t>microarray.</t> ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.
Ultra Thin, Nitrocellulose Coated Microscope Slides Path Slides, supplied by GenTel BioSurfaces, 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/result/ultra-thin, nitrocellulose-coated microscope slides path slides/product/GenTel BioSurfaces
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ultra-thin, nitrocellulose-coated microscope slides path slides - by Bioz Stars, 2026-06
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nexterion® slide h  (SCHOTT)
90
SCHOTT nexterion® slide h
Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen <t>microarray.</t> ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.
Nexterion® Slide H, supplied by SCHOTT, 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/result/nexterion® slide h/product/SCHOTT
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nexterion® slide h - by Bioz Stars, 2026-06
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sciflexarrayer s1  (SCIENION)
95
SCIENION sciflexarrayer s1
Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen <t>microarray.</t> ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.
Sciflexarrayer S1, 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
https://www.bioz.com/result/sciflexarrayer s1/product/SCIENION
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sciflexarrayer s1 - by Bioz Stars, 2026-06
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aldehyde-modified glass slides nexterion slides al  (PEQLAB)
90
PEQLAB aldehyde-modified glass slides nexterion slides al
Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen <t>microarray.</t> ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.
Aldehyde Modified Glass Slides Nexterion Slides Al, supplied by PEQLAB, 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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epoxy microarray slides nexterion slide e  (SCHOTT)
90
SCHOTT epoxy microarray slides nexterion slide e
<t> Lectins </t> used in microarray; their glycan specificity and reactivity with a PD transferrin (weak “+” and strong “++”).
Epoxy Microarray Slides Nexterion Slide E, supplied by SCHOTT, 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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epoxy microarray slides nexterion slide e - by Bioz Stars, 2026-06
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masked-well glass slides coated with teflon/epoxy-silane  (Tekdon Inc)
90
Tekdon Inc masked-well glass slides coated with teflon/epoxy-silane
<t> Lectins </t> used in microarray; their glycan specificity and reactivity with a PD transferrin (weak “+” and strong “++”).
Masked Well Glass Slides Coated With Teflon/Epoxy Silane, supplied by Tekdon Inc, 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/result/masked-well glass slides coated with teflon/epoxy-silane/product/Tekdon Inc
Average 90 stars, based on 1 article reviews
masked-well glass slides coated with teflon/epoxy-silane - by Bioz Stars, 2026-06
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Image Search Results


Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen microarray. ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.

Journal: Microbiology Spectrum

Article Title: Nanobody engineering for SARS-CoV-2 neutralization and detection

doi: 10.1128/spectrum.04199-22

Figure Lengend Snippet: Relative binding strengths of trimeric nanobodies to RBD and Spike S1 domain variants on an antigen microarray. ( A ) Three multimodular nanobody constructs were tested for binding to RBD variants with amino acid changes K417N, E484K, or N501Y, and to spike the S1 domain with four amino acid changes (K417N, E484K, N501Y, and D614G). Fluorescence signals of Dylight 633-labeled multimodular nanobodies Tri-Ty1, Tri-TMH, and Tri-TMV bound to the different RBD and S1 variants are shown normalized relative to the signal from binding to wild-type RBD or S1 for each nanobody, respectively. Error bars represent the standard deviation of two replicate measurements. ( B ) Location of the amino acid changes within the SARS-CoV-2 RBD. Amino acid change N501Y is found in the Alpha and Beta variants ( , ), and the Beta variant displays the additional changes K417N and E484K . Delta variant carries none of the three tested RBD amino acid changes, while Omicron displays N501Y, K417N, and an alternative change at residue 484, E484A.

Article Snippet: Wild-type and variant SARS-CoV-2 RBD and spike S1 domains were biotinylated and arrayed as duplicate spots (0.1 ng per spot) in the wells of streptavidin-coated microtitration plates using a piezoelectric non-contact microarray dispenser (Nano-Plotter, GeSiM, Germany).

Techniques: Binding Assay, Microarray, Construct, Fluorescence, Labeling, Standard Deviation, Variant Assay, Residue

Lectins used in microarray; their glycan specificity and reactivity with a PD transferrin (weak “+” and strong “++”).

Journal: International Journal of Molecular Sciences

Article Title: Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease

doi: 10.3390/ijms25094625

Figure Lengend Snippet: Lectins used in microarray; their glycan specificity and reactivity with a PD transferrin (weak “+” and strong “++”).

Article Snippet: A microarray analysis was performed with each sample separately using biotinylated lectins, epoxy microarray slides (NEXTERION Slide E, Schott, Germany), a non-contact piezoelectric sciFLEXARRAYER S1 microarray spotter and a piezo dispense capillary PDC 80 (Scienion AG, Berlin, Germany) [ ].

Techniques: Microarray, Glycoproteomics, Whole Genome Amplification

Reactivity of transferrin isolated from healthy persons (H) and patients on peritoneal dialysis (PD) with lectins. A statistically significant difference between groups ( p < 0.05) is labeled with “*”.

Journal: International Journal of Molecular Sciences

Article Title: Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease

doi: 10.3390/ijms25094625

Figure Lengend Snippet: Reactivity of transferrin isolated from healthy persons (H) and patients on peritoneal dialysis (PD) with lectins. A statistically significant difference between groups ( p < 0.05) is labeled with “*”.

Article Snippet: A microarray analysis was performed with each sample separately using biotinylated lectins, epoxy microarray slides (NEXTERION Slide E, Schott, Germany), a non-contact piezoelectric sciFLEXARRAYER S1 microarray spotter and a piezo dispense capillary PDC 80 (Scienion AG, Berlin, Germany) [ ].

Techniques: Isolation, Labeling