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Arrayit Corporation glycan microarray slides
A Relative fluorescence unit (RFU) of F598 mAb binding with the library of 32 PNAG pentasaccharides. The glycans are grouped according to the number of NHAc units in the molecule. Each PNAG sequence is printed five times on the glycan <t>microarray.</t> The error bars represent the standard deviations of five individual spots. Data are presented as mean values ± standard deviation. F598 generally prefers highly acetylated PNAG sequences. Both the location and the number of NHAc units are important determinants of F598 binding. B Quantification of the preference of F598 for acetylation at each site of the PNAG pentasaccharide. The mean values are calculated from the values of the binding intensities of all 32 PNAG sequences to F598. Each PNAG sequence is printed five times on the glycan microarray. Data are presented as mean values ± standard deviation. Source data are provided as a file.
Glycan Microarray Slides, supplied by Arrayit 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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1) Product Images from "A comprehensive synthetic library of poly- N -acetyl glucosamines enabled vaccine against lethal challenges of Staphylococcus aureus"

Article Title: A comprehensive synthetic library of poly- N -acetyl glucosamines enabled vaccine against lethal challenges of Staphylococcus aureus

Journal: Nature Communications

doi: 10.1038/s41467-024-47457-4

A Relative fluorescence unit (RFU) of F598 mAb binding with the library of 32 PNAG pentasaccharides. The glycans are grouped according to the number of NHAc units in the molecule. Each PNAG sequence is printed five times on the glycan microarray. The error bars represent the standard deviations of five individual spots. Data are presented as mean values ± standard deviation. F598 generally prefers highly acetylated PNAG sequences. Both the location and the number of NHAc units are important determinants of F598 binding. B Quantification of the preference of F598 for acetylation at each site of the PNAG pentasaccharide. The mean values are calculated from the values of the binding intensities of all 32 PNAG sequences to F598. Each PNAG sequence is printed five times on the glycan microarray. Data are presented as mean values ± standard deviation. Source data are provided as a file.
Figure Legend Snippet: A Relative fluorescence unit (RFU) of F598 mAb binding with the library of 32 PNAG pentasaccharides. The glycans are grouped according to the number of NHAc units in the molecule. Each PNAG sequence is printed five times on the glycan microarray. The error bars represent the standard deviations of five individual spots. Data are presented as mean values ± standard deviation. F598 generally prefers highly acetylated PNAG sequences. Both the location and the number of NHAc units are important determinants of F598 binding. B Quantification of the preference of F598 for acetylation at each site of the PNAG pentasaccharide. The mean values are calculated from the values of the binding intensities of all 32 PNAG sequences to F598. Each PNAG sequence is printed five times on the glycan microarray. Data are presented as mean values ± standard deviation. Source data are provided as a file.

Techniques Used: Fluorescence, Binding Assay, Sequencing, Glycoproteomics, Microarray, Standard Deviation

A IgG antibody titers to the immunizing PNAG oligosaccharide in rabbit ( n = 2 per group) sera on day 35 after prime vaccination. B IgG antibody titers in pooled rabbit sera from mQβ-conjugate or 5GlcNH 2 –TT conjugate immunized animals ( n = 2 per group) as well as titer of natural human IgG in pooled human serum against native PNAG polysaccharide purified from Acinetobacter baumannii . The numbers above symbols are the average titer numbers. Titers and 95% confidence intervals (CI) were determined by linear regression using log 10 values of the average of replicate serum dilutions to determine the X intercept and 95% CI when Y = 0.5 (OD 405 nm of ELISA plate reading). C Stacked bar graphs depicting the IgG signals at the serum dilution of 1:50,000 for each rabbit ( n = 2) immunized with mQβ–PNAG0, mQβ–PNAG10, and mQβ–PNAG26 as well as pre-immune sera, respectively, on the array. The complete microarray results are provided in the file; D Normalized binding of the comprehensive library of PNAG pentasaccharides by IgG antibodies from post-immune sera of rabbits immunized with mQβ–PNAG0, mQβ–PNAG10, and mQβ–PNAG26, respectively, as well as pre-immune sera. PNAG sequences are grouped together according to the total number of acetamides in the molecules. The color scale bar is shown on the right with 100% indicating the strongest binding to a PNAG component and 0% indicating the weakest binder. For each antigen, the two rows represent sera from two rabbits per group immunized with the specific construct. Source data are provided as a file.
Figure Legend Snippet: A IgG antibody titers to the immunizing PNAG oligosaccharide in rabbit ( n = 2 per group) sera on day 35 after prime vaccination. B IgG antibody titers in pooled rabbit sera from mQβ-conjugate or 5GlcNH 2 –TT conjugate immunized animals ( n = 2 per group) as well as titer of natural human IgG in pooled human serum against native PNAG polysaccharide purified from Acinetobacter baumannii . The numbers above symbols are the average titer numbers. Titers and 95% confidence intervals (CI) were determined by linear regression using log 10 values of the average of replicate serum dilutions to determine the X intercept and 95% CI when Y = 0.5 (OD 405 nm of ELISA plate reading). C Stacked bar graphs depicting the IgG signals at the serum dilution of 1:50,000 for each rabbit ( n = 2) immunized with mQβ–PNAG0, mQβ–PNAG10, and mQβ–PNAG26 as well as pre-immune sera, respectively, on the array. The complete microarray results are provided in the file; D Normalized binding of the comprehensive library of PNAG pentasaccharides by IgG antibodies from post-immune sera of rabbits immunized with mQβ–PNAG0, mQβ–PNAG10, and mQβ–PNAG26, respectively, as well as pre-immune sera. PNAG sequences are grouped together according to the total number of acetamides in the molecules. The color scale bar is shown on the right with 100% indicating the strongest binding to a PNAG component and 0% indicating the weakest binder. For each antigen, the two rows represent sera from two rabbits per group immunized with the specific construct. Source data are provided as a file.

Techniques Used: Purification, Enzyme-linked Immunosorbent Assay, Microarray, Binding Assay, Construct

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Article Snippet: .. Sialoglycan Microarray Fabrication Arrays were fabricated with NanoPrint LM-60 Microarray Printer (Arrayit) on epoxide-derivatized slides (Corning) with 16 subarray blocks on each slide. ..

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Produced:

Article Title: A comprehensive synthetic library of poly-N-acetyl glucosamines enabled vaccine against lethal challenges of Staphylococcus aureus.
Article Snippet: .. Glycanmicroarray slideswere produced aspreviously described44,45 on SuperEpoxy 2 slides (SME2; ArrayIt Corp, Sunnyvale, CA) and stored vacuum sealed at −20 °C. ..

Article Title: A comprehensive synthetic library of poly- N -acetyl glucosamines enabled vaccine against lethal challenges of Staphylococcus aureus
Article Snippet: .. Glycan microarray slides were produced as previously described , on SuperEpoxy 2 slides (SME2; ArrayIt Corp, Sunnyvale, CA) and stored vacuum sealed at −20 °C. ..

other:

Article Title: Synthesis of Asymmetric N -Glycans as Common Core Substrates for Structural Diversification through Selective Enzymatic Glycosylation.
Article Snippet: N-glycans on the cell surface provide distinct signatures that are recognized by different glycan-binding proteins (GBPs) and pathogens.. Most glycans in humans are asymmetric and isomeric, yet their biological functions are not well understood due to their lack of availability for studies.. In this work, we have developed an improved strategy for asymmetric N-glycan assembly and diversification using designed common core substrates prepared chemically for selective enzymatic fucosylation and sialylation.

Glycoproteomics:

Article Title: Identification of the Glycan Binding Profile of Human and Rodent Plasmodium Sporozoites.
Article Snippet: The transmission of Plasmodium spp. sporozoites to the mammalian host is the first step in the initiation of the mosquito-borne disease known as malaria.. The exact route of transmission from the bloodstream to the liver is still not clearly elucidated, and identification of the host glycan structures bound by the sporozoites may inform as to which host cells are involved.. Here, we provide a comprehensive analysis of the glycan structures that sporozoites from the human pathogen, P. falciparum, and the rodent pathogen, P. yoelii, recognize and bind.

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Article Title: Subtilase cytotoxin B subunit mutant
Article Snippet: .. For the data shown in Table 3, glycan array slides were printed on SuperEpoxy 3 (Arrayit) activated substrates using an Arrayit Spotbot Extreme contact printer as previously described28. .. For each subarray 2 μg of SubB proteins were pre-complexed with anti-His tag antibody (Cell signalling) and Alexa555 secondary and tertiary antibodies (rabbit anti-mouse; goat anti-rabbit) at a ratio of 2:1:0.5:0.25 in a final volume of 500 μL.

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Article Snippet: .. The differences may be explained 186 by the different surface chemistries of the CFG (Schott Nexterion NHS 3D polymer 187 substrates) and the glycan array used in this study (ArrayIt SuperEpoxy II 2D 188 activated silicon surface). ..

Article Title: A comprehensive synthetic library of poly- N -acetyl glucosamines enabled vaccine against lethal challenges of Staphylococcus aureus
Article Snippet: .. Glycan microarray slides were produced as previously described , on SuperEpoxy 2 slides (SME2; ArrayIt Corp, Sunnyvale, CA) and stored vacuum sealed at −20 °C. ..

Centrifugation:

Article Title: Identification of the Glycan Binding Profile of Human and Rodent Plasmodium Sporozoites.
Article Snippet: The transmission of Plasmodium spp. sporozoites to the mammalian host is the first step in the initiation of the mosquito-borne disease known as malaria.. The exact route of transmission from the bloodstream to the liver is still not clearly elucidated, and identification of the host glycan structures bound by the sporozoites may inform as to which host cells are involved.. Here, we provide a comprehensive analysis of the glycan structures that sporozoites from the human pathogen, P. falciparum, and the rodent pathogen, P. yoelii, recognize and bind.

Labeling:

Article Title: Identification of the Glycan Binding Profile of Human and Rodent Plasmodium Sporozoites.
Article Snippet: The transmission of Plasmodium spp. sporozoites to the mammalian host is the first step in the initiation of the mosquito-borne disease known as malaria.. The exact route of transmission from the bloodstream to the liver is still not clearly elucidated, and identification of the host glycan structures bound by the sporozoites may inform as to which host cells are involved.. Here, we provide a comprehensive analysis of the glycan structures that sporozoites from the human pathogen, P. falciparum, and the rodent pathogen, P. yoelii, recognize and bind.

Hybridization:

Article Title: Equine and Canine Influenza H3N8 Viruses Show Minimal Biological Differences Despite Phylogenetic Divergence
Article Snippet: .. Briefly, freshly printed glycan microarray slides were blocked by ethanolamine, washed and dried, and then fitted in a multiwell microarray hybridization cassette (ArrayIt, CA) to divide them into subarrays. ..

Polymer:

Article Title: Lectin Activity of the TcdA and TcdB Toxins of Clostridium difficile
Article Snippet: .. The differences may be explained 186 by the different surface chemistries of the CFG (Schott Nexterion NHS 3D polymer 187 substrates) and the glycan array used in this study (ArrayIt SuperEpoxy II 2D 188 activated silicon surface). ..



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A Relative fluorescence unit (RFU) of F598 mAb binding with the library of 32 PNAG pentasaccharides. The glycans are grouped according to the number of NHAc units in the molecule. Each PNAG sequence is printed five times on the glycan <t>microarray.</t> The error bars represent the standard deviations of five individual spots. Data are presented as mean values ± standard deviation. F598 generally prefers highly acetylated PNAG sequences. Both the location and the number of NHAc units are important determinants of F598 binding. B Quantification of the preference of F598 for acetylation at each site of the PNAG pentasaccharide. The mean values are calculated from the values of the binding intensities of all 32 PNAG sequences to F598. Each PNAG sequence is printed five times on the glycan microarray. Data are presented as mean values ± standard deviation. Source data are provided as a file.
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Image Search Results


A Relative fluorescence unit (RFU) of F598 mAb binding with the library of 32 PNAG pentasaccharides. The glycans are grouped according to the number of NHAc units in the molecule. Each PNAG sequence is printed five times on the glycan microarray. The error bars represent the standard deviations of five individual spots. Data are presented as mean values ± standard deviation. F598 generally prefers highly acetylated PNAG sequences. Both the location and the number of NHAc units are important determinants of F598 binding. B Quantification of the preference of F598 for acetylation at each site of the PNAG pentasaccharide. The mean values are calculated from the values of the binding intensities of all 32 PNAG sequences to F598. Each PNAG sequence is printed five times on the glycan microarray. Data are presented as mean values ± standard deviation. Source data are provided as a file.

Journal: Nature Communications

Article Title: A comprehensive synthetic library of poly- N -acetyl glucosamines enabled vaccine against lethal challenges of Staphylococcus aureus

doi: 10.1038/s41467-024-47457-4

Figure Lengend Snippet: A Relative fluorescence unit (RFU) of F598 mAb binding with the library of 32 PNAG pentasaccharides. The glycans are grouped according to the number of NHAc units in the molecule. Each PNAG sequence is printed five times on the glycan microarray. The error bars represent the standard deviations of five individual spots. Data are presented as mean values ± standard deviation. F598 generally prefers highly acetylated PNAG sequences. Both the location and the number of NHAc units are important determinants of F598 binding. B Quantification of the preference of F598 for acetylation at each site of the PNAG pentasaccharide. The mean values are calculated from the values of the binding intensities of all 32 PNAG sequences to F598. Each PNAG sequence is printed five times on the glycan microarray. Data are presented as mean values ± standard deviation. Source data are provided as a file.

Article Snippet: Glycan microarray slides were produced as previously described , on SuperEpoxy 2 slides (SME2; ArrayIt Corp, Sunnyvale, CA) and stored vacuum sealed at −20 °C.

Techniques: Fluorescence, Binding Assay, Sequencing, Glycoproteomics, Microarray, Standard Deviation

A IgG antibody titers to the immunizing PNAG oligosaccharide in rabbit ( n = 2 per group) sera on day 35 after prime vaccination. B IgG antibody titers in pooled rabbit sera from mQβ-conjugate or 5GlcNH 2 –TT conjugate immunized animals ( n = 2 per group) as well as titer of natural human IgG in pooled human serum against native PNAG polysaccharide purified from Acinetobacter baumannii . The numbers above symbols are the average titer numbers. Titers and 95% confidence intervals (CI) were determined by linear regression using log 10 values of the average of replicate serum dilutions to determine the X intercept and 95% CI when Y = 0.5 (OD 405 nm of ELISA plate reading). C Stacked bar graphs depicting the IgG signals at the serum dilution of 1:50,000 for each rabbit ( n = 2) immunized with mQβ–PNAG0, mQβ–PNAG10, and mQβ–PNAG26 as well as pre-immune sera, respectively, on the array. The complete microarray results are provided in the file; D Normalized binding of the comprehensive library of PNAG pentasaccharides by IgG antibodies from post-immune sera of rabbits immunized with mQβ–PNAG0, mQβ–PNAG10, and mQβ–PNAG26, respectively, as well as pre-immune sera. PNAG sequences are grouped together according to the total number of acetamides in the molecules. The color scale bar is shown on the right with 100% indicating the strongest binding to a PNAG component and 0% indicating the weakest binder. For each antigen, the two rows represent sera from two rabbits per group immunized with the specific construct. Source data are provided as a file.

Journal: Nature Communications

Article Title: A comprehensive synthetic library of poly- N -acetyl glucosamines enabled vaccine against lethal challenges of Staphylococcus aureus

doi: 10.1038/s41467-024-47457-4

Figure Lengend Snippet: A IgG antibody titers to the immunizing PNAG oligosaccharide in rabbit ( n = 2 per group) sera on day 35 after prime vaccination. B IgG antibody titers in pooled rabbit sera from mQβ-conjugate or 5GlcNH 2 –TT conjugate immunized animals ( n = 2 per group) as well as titer of natural human IgG in pooled human serum against native PNAG polysaccharide purified from Acinetobacter baumannii . The numbers above symbols are the average titer numbers. Titers and 95% confidence intervals (CI) were determined by linear regression using log 10 values of the average of replicate serum dilutions to determine the X intercept and 95% CI when Y = 0.5 (OD 405 nm of ELISA plate reading). C Stacked bar graphs depicting the IgG signals at the serum dilution of 1:50,000 for each rabbit ( n = 2) immunized with mQβ–PNAG0, mQβ–PNAG10, and mQβ–PNAG26 as well as pre-immune sera, respectively, on the array. The complete microarray results are provided in the file; D Normalized binding of the comprehensive library of PNAG pentasaccharides by IgG antibodies from post-immune sera of rabbits immunized with mQβ–PNAG0, mQβ–PNAG10, and mQβ–PNAG26, respectively, as well as pre-immune sera. PNAG sequences are grouped together according to the total number of acetamides in the molecules. The color scale bar is shown on the right with 100% indicating the strongest binding to a PNAG component and 0% indicating the weakest binder. For each antigen, the two rows represent sera from two rabbits per group immunized with the specific construct. Source data are provided as a file.

Article Snippet: Glycan microarray slides were produced as previously described , on SuperEpoxy 2 slides (SME2; ArrayIt Corp, Sunnyvale, CA) and stored vacuum sealed at −20 °C.

Techniques: Purification, Enzyme-linked Immunosorbent Assay, Microarray, Binding Assay, Construct