superstreptavidin microarray substrate slides Search Results


96
SCIENION sciflexarrayer s3 noncontact microarray
Probing the substrate tolerance of Clostridium perfringens sialidases using the acetylated sialosides <t>microarray.</t> The acetylated sialosides array was treated with NanH GH33 , NanI GH33 , and NanJ GH33 (20 μg/ml in pH 7.4 PBS buffer) at 37 °C for 1 h. Bovine coronavirus hemagglutinin-esterase (BCoV HE) was then used to probe the result of the sialidase treatment. Loss of binding signal after sialidase treatment suggests cleavage of the sialic acid. Microarray data for the untreated control and the NanH GH33 , NanI GH33 , and NanJ GH33 treated slides are shown for ( A ) acetylated 2,3-sialosides, ( B ) acetylated 2,6-sialosides, and ( C ) acetylated 2,8-sialosides. Data are shown as quadruplicate values, with the error bar representing standard deviation of the mean. D , summary of substrate tolerance of the sialidase on the acetylated sialosides.
Sciflexarrayer S3 Noncontact Microarray, 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
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86
Biacore biacore t100 evaluation software
Probing the substrate tolerance of Clostridium perfringens sialidases using the acetylated sialosides <t>microarray.</t> The acetylated sialosides array was treated with NanH GH33 , NanI GH33 , and NanJ GH33 (20 μg/ml in pH 7.4 PBS buffer) at 37 °C for 1 h. Bovine coronavirus hemagglutinin-esterase (BCoV HE) was then used to probe the result of the sialidase treatment. Loss of binding signal after sialidase treatment suggests cleavage of the sialic acid. Microarray data for the untreated control and the NanH GH33 , NanI GH33 , and NanJ GH33 treated slides are shown for ( A ) acetylated 2,3-sialosides, ( B ) acetylated 2,6-sialosides, and ( C ) acetylated 2,8-sialosides. Data are shown as quadruplicate values, with the error bar representing standard deviation of the mean. D , summary of substrate tolerance of the sialidase on the acetylated sialosides.
Biacore T100 Evaluation Software, supplied by Biacore, 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/result/biacore t100 evaluation software/product/Biacore
Average 86 stars, based on 1 article reviews
biacore t100 evaluation software - by Bioz Stars, 2026-06
86/100 stars
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Probing the substrate tolerance of Clostridium perfringens sialidases using the acetylated sialosides microarray. The acetylated sialosides array was treated with NanH GH33 , NanI GH33 , and NanJ GH33 (20 μg/ml in pH 7.4 PBS buffer) at 37 °C for 1 h. Bovine coronavirus hemagglutinin-esterase (BCoV HE) was then used to probe the result of the sialidase treatment. Loss of binding signal after sialidase treatment suggests cleavage of the sialic acid. Microarray data for the untreated control and the NanH GH33 , NanI GH33 , and NanJ GH33 treated slides are shown for ( A ) acetylated 2,3-sialosides, ( B ) acetylated 2,6-sialosides, and ( C ) acetylated 2,8-sialosides. Data are shown as quadruplicate values, with the error bar representing standard deviation of the mean. D , summary of substrate tolerance of the sialidase on the acetylated sialosides.

Journal: The Journal of Biological Chemistry

Article Title: A “terminal” case of glycan catabolism: Structural and enzymatic characterization of the sialidases of Clostridium perfringens

doi: 10.1016/j.jbc.2024.107750

Figure Lengend Snippet: Probing the substrate tolerance of Clostridium perfringens sialidases using the acetylated sialosides microarray. The acetylated sialosides array was treated with NanH GH33 , NanI GH33 , and NanJ GH33 (20 μg/ml in pH 7.4 PBS buffer) at 37 °C for 1 h. Bovine coronavirus hemagglutinin-esterase (BCoV HE) was then used to probe the result of the sialidase treatment. Loss of binding signal after sialidase treatment suggests cleavage of the sialic acid. Microarray data for the untreated control and the NanH GH33 , NanI GH33 , and NanJ GH33 treated slides are shown for ( A ) acetylated 2,3-sialosides, ( B ) acetylated 2,6-sialosides, and ( C ) acetylated 2,8-sialosides. Data are shown as quadruplicate values, with the error bar representing standard deviation of the mean. D , summary of substrate tolerance of the sialidase on the acetylated sialosides.

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

Techniques: Microarray, Binding Assay, Control, Standard Deviation

Assessing the tolerance of C. perfringens sialidases against O -acetylated sialic acids. A – L , release of O -acetylated sialic acid species indicated in the panels by each enzyme. Bovine submaxillary mucin (BSM) was treated with NanI GH33 , NanJ GH33 , and NanH GH33 for 5.5 h after which liberated sialic acids were derivatized and analyzed by HPLC-MS. Activities of each sialidase were normalized based on their rate of hydrolyzing 4MU-Neu5Ac. Three replicates were assessed per sialidase, with error bars representing the standard deviation of the mean. In all instances, MS detector responses for each unique sialic acid were normalized to the total detectible sialic acid pool in each sample. Except for Neu5Ac, Neu5Gc, and Neu5,9Ac 2 , all assignments are putative albeit Neu5,7Ac2, Neu5,8Ac2 (and their Neu5Gc congeners) are consistent with their previously reported retention times and fragmentation patterns. In E - G , triacetylated substrates at four positions (5 and 7/8/9) were not confidently identified and are thus listed as Neu5,7/8/9_1, _2, and _3. Based on microarray data , we propose what we have annotated as Neu5,7/8/9Ac3_3 is Neu5,7,9Ac3. Neu5Ac, N -acetylneuraminic acid; Neu5Gc, N -glycolylneuraminic acid; HPLC-MS, high-performance liquid chromatography coupled to mass spectrometry.

Journal: The Journal of Biological Chemistry

Article Title: A “terminal” case of glycan catabolism: Structural and enzymatic characterization of the sialidases of Clostridium perfringens

doi: 10.1016/j.jbc.2024.107750

Figure Lengend Snippet: Assessing the tolerance of C. perfringens sialidases against O -acetylated sialic acids. A – L , release of O -acetylated sialic acid species indicated in the panels by each enzyme. Bovine submaxillary mucin (BSM) was treated with NanI GH33 , NanJ GH33 , and NanH GH33 for 5.5 h after which liberated sialic acids were derivatized and analyzed by HPLC-MS. Activities of each sialidase were normalized based on their rate of hydrolyzing 4MU-Neu5Ac. Three replicates were assessed per sialidase, with error bars representing the standard deviation of the mean. In all instances, MS detector responses for each unique sialic acid were normalized to the total detectible sialic acid pool in each sample. Except for Neu5Ac, Neu5Gc, and Neu5,9Ac 2 , all assignments are putative albeit Neu5,7Ac2, Neu5,8Ac2 (and their Neu5Gc congeners) are consistent with their previously reported retention times and fragmentation patterns. In E - G , triacetylated substrates at four positions (5 and 7/8/9) were not confidently identified and are thus listed as Neu5,7/8/9_1, _2, and _3. Based on microarray data , we propose what we have annotated as Neu5,7/8/9Ac3_3 is Neu5,7,9Ac3. Neu5Ac, N -acetylneuraminic acid; Neu5Gc, N -glycolylneuraminic acid; HPLC-MS, high-performance liquid chromatography coupled to mass spectrometry.

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

Techniques: Standard Deviation, Microarray, High Performance Liquid Chromatography, Mass Spectrometry