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pna biotin  (Vector Laboratories)


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    Vector Laboratories pna biotin
    Pna Biotin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 143 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pna biotin/product/Vector Laboratories
    Average 93 stars, based on 143 article reviews
    pna biotin - by Bioz Stars, 2026-03
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    Overview of the study of GalNAc-type O-glycosylation in neuronal tissues. A , schematic of common O-glycan structures found in the mammalian brain . The most abundant di-sialyl-T (DiST) structure is biosynthesized from the underlying Core one structure. Only a minor fraction of the Core two structure was reported. A combination of desialylation (Neu) and Core 1- (Jacalin and Peanut agglutinin, PNA) or Tn- ( Vicia villosa , <t>VVA)</t> <t>binding</t> <t>lectins</t> was used to enrich for tryptic glycopeptides subjected to our glycoproteomic workflow (Sfig 1A). B , Bar graph displaying the number of glycoproteins and glycosites identified from individual biosources across species. C , overview of the expanded neuronal glycoproteome built by consolidating human O-glycosites with animal sites that are conserved in human proteins by orthologue sequence alignment (3389 sites). Sequence alignment was performed using ClustalO on the full-length sequence of each animal glycoprotein and its human orthologue. Glycosites that aligned to Ser/Thr/Tyr were included in the expanded neuronal glycoproteome (4228) ( bottom ). Proportion of human sites, expanding sites and total number of sites predicted by the Net-O-Glyc 4.0 algorithm are stated in parentheses. D , species source overlap among the total 4228 O-glycosites of the expanded dataset. E , the expanded neuronal O-glycoproteome contributes novel O-glycosites compared to the current aggregate of experimentally identified human O-glycosites ( yellow ) ( https://glyco.me/docs/resources/glycodomain/ ). The proportion of sites that are experimentally verified in human samples is given in parentheses.
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    Overview of the study of GalNAc-type O-glycosylation in neuronal tissues. A , schematic of common O-glycan structures found in the mammalian brain . The most abundant di-sialyl-T (DiST) structure is biosynthesized from the underlying Core one structure. Only a minor fraction of the Core two structure was reported. A combination of desialylation (Neu) and Core 1- (Jacalin and Peanut agglutinin, PNA) or Tn- ( Vicia villosa , <t>VVA)</t> <t>binding</t> <t>lectins</t> was used to enrich for tryptic glycopeptides subjected to our glycoproteomic workflow (Sfig 1A). B , Bar graph displaying the number of glycoproteins and glycosites identified from individual biosources across species. C , overview of the expanded neuronal glycoproteome built by consolidating human O-glycosites with animal sites that are conserved in human proteins by orthologue sequence alignment (3389 sites). Sequence alignment was performed using ClustalO on the full-length sequence of each animal glycoprotein and its human orthologue. Glycosites that aligned to Ser/Thr/Tyr were included in the expanded neuronal glycoproteome (4228) ( bottom ). Proportion of human sites, expanding sites and total number of sites predicted by the Net-O-Glyc 4.0 algorithm are stated in parentheses. D , species source overlap among the total 4228 O-glycosites of the expanded dataset. E , the expanded neuronal O-glycoproteome contributes novel O-glycosites compared to the current aggregate of experimentally identified human O-glycosites ( yellow ) ( https://glyco.me/docs/resources/glycodomain/ ). The proportion of sites that are experimentally verified in human samples is given in parentheses.
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    Overview of the study of GalNAc-type O-glycosylation in neuronal tissues. A , schematic of common O-glycan structures found in the mammalian brain . The most abundant di-sialyl-T (DiST) structure is biosynthesized from the underlying Core one structure. Only a minor fraction of the Core two structure was reported. A combination of desialylation (Neu) and Core 1- (Jacalin and Peanut agglutinin, PNA) or Tn- ( Vicia villosa , VVA) binding lectins was used to enrich for tryptic glycopeptides subjected to our glycoproteomic workflow (Sfig 1A). B , Bar graph displaying the number of glycoproteins and glycosites identified from individual biosources across species. C , overview of the expanded neuronal glycoproteome built by consolidating human O-glycosites with animal sites that are conserved in human proteins by orthologue sequence alignment (3389 sites). Sequence alignment was performed using ClustalO on the full-length sequence of each animal glycoprotein and its human orthologue. Glycosites that aligned to Ser/Thr/Tyr were included in the expanded neuronal glycoproteome (4228) ( bottom ). Proportion of human sites, expanding sites and total number of sites predicted by the Net-O-Glyc 4.0 algorithm are stated in parentheses. D , species source overlap among the total 4228 O-glycosites of the expanded dataset. E , the expanded neuronal O-glycoproteome contributes novel O-glycosites compared to the current aggregate of experimentally identified human O-glycosites ( yellow ) ( https://glyco.me/docs/resources/glycodomain/ ). The proportion of sites that are experimentally verified in human samples is given in parentheses.

    Journal: The Journal of Biological Chemistry

    Article Title: Map of the neuronal O-glycoproteome reveals driver functions in the regulated secretory pathway

    doi: 10.1016/j.jbc.2025.110313

    Figure Lengend Snippet: Overview of the study of GalNAc-type O-glycosylation in neuronal tissues. A , schematic of common O-glycan structures found in the mammalian brain . The most abundant di-sialyl-T (DiST) structure is biosynthesized from the underlying Core one structure. Only a minor fraction of the Core two structure was reported. A combination of desialylation (Neu) and Core 1- (Jacalin and Peanut agglutinin, PNA) or Tn- ( Vicia villosa , VVA) binding lectins was used to enrich for tryptic glycopeptides subjected to our glycoproteomic workflow (Sfig 1A). B , Bar graph displaying the number of glycoproteins and glycosites identified from individual biosources across species. C , overview of the expanded neuronal glycoproteome built by consolidating human O-glycosites with animal sites that are conserved in human proteins by orthologue sequence alignment (3389 sites). Sequence alignment was performed using ClustalO on the full-length sequence of each animal glycoprotein and its human orthologue. Glycosites that aligned to Ser/Thr/Tyr were included in the expanded neuronal glycoproteome (4228) ( bottom ). Proportion of human sites, expanding sites and total number of sites predicted by the Net-O-Glyc 4.0 algorithm are stated in parentheses. D , species source overlap among the total 4228 O-glycosites of the expanded dataset. E , the expanded neuronal O-glycoproteome contributes novel O-glycosites compared to the current aggregate of experimentally identified human O-glycosites ( yellow ) ( https://glyco.me/docs/resources/glycodomain/ ). The proportion of sites that are experimentally verified in human samples is given in parentheses.

    Article Snippet: Subsequently, blots were incubated O/N using the following lectins or antibodies: VVA-Biotin 1:2000 (Vector-labs, B-1235–2), PNA-Biotin 1:2000 (Vector-labs, B-1075–5), Anti-CHGA 1:1000 (AbCam, Ab15160), Anti-CS 1:1000 (Abcam, ab11570), Anti-B-actin 1:10.000 (Protein Tech, 66009-1-Ig), anti-CHGB (Abcam, ab12242) or anti-VGF (Abcam, ab69989).

    Techniques: Glycoproteomics, Binding Assay, Sequencing

    Probing roles of elaborate O-glycans for regulated secre tion . A , targeting C1GALT1 enzyme or its obligate private COSMC chaperone by CRISPR-Cas9 results in SC cells producing truncated (Tn) O-glycans on proteins. B , representative immunofluorescence images of STC-1 and SH-SY5Y WT and SC cells. Pretreatment with neuraminidase shows the gain of Tn (VVA) and loss of Core 1 (PNA) in SCs and validates the glycoengineering. C and D , Western blot analysis of secretomes ± depolarization from SH-SY5Y and STC-1 WT and SC cells. Blots were pretreated with neuraminidase and probed with the VVA lectin to selectively identify O-glycoproteins with truncated Tn O-glycans. Arrows indicate relative migration of highly glycosylated granins (deferred from separate western blots (Sfig 2C)). A VVA-reactive smear that co-mobilizes with both chondroitin sulfate and high molecular weight CHGA is indicated by a grey arrow . Asterisks (∗) denote background bands. E , Bar plot showing the mean relative secretion of the KCl-responsive proteins in SH-SY5Y WT and ΔCOSMC (SH-SY5Y SC ). Error bars represent + standard error of the mean, n = 5 clones.

    Journal: The Journal of Biological Chemistry

    Article Title: Map of the neuronal O-glycoproteome reveals driver functions in the regulated secretory pathway

    doi: 10.1016/j.jbc.2025.110313

    Figure Lengend Snippet: Probing roles of elaborate O-glycans for regulated secre tion . A , targeting C1GALT1 enzyme or its obligate private COSMC chaperone by CRISPR-Cas9 results in SC cells producing truncated (Tn) O-glycans on proteins. B , representative immunofluorescence images of STC-1 and SH-SY5Y WT and SC cells. Pretreatment with neuraminidase shows the gain of Tn (VVA) and loss of Core 1 (PNA) in SCs and validates the glycoengineering. C and D , Western blot analysis of secretomes ± depolarization from SH-SY5Y and STC-1 WT and SC cells. Blots were pretreated with neuraminidase and probed with the VVA lectin to selectively identify O-glycoproteins with truncated Tn O-glycans. Arrows indicate relative migration of highly glycosylated granins (deferred from separate western blots (Sfig 2C)). A VVA-reactive smear that co-mobilizes with both chondroitin sulfate and high molecular weight CHGA is indicated by a grey arrow . Asterisks (∗) denote background bands. E , Bar plot showing the mean relative secretion of the KCl-responsive proteins in SH-SY5Y WT and ΔCOSMC (SH-SY5Y SC ). Error bars represent + standard error of the mean, n = 5 clones.

    Article Snippet: Subsequently, blots were incubated O/N using the following lectins or antibodies: VVA-Biotin 1:2000 (Vector-labs, B-1235–2), PNA-Biotin 1:2000 (Vector-labs, B-1075–5), Anti-CHGA 1:1000 (AbCam, Ab15160), Anti-CS 1:1000 (Abcam, ab11570), Anti-B-actin 1:10.000 (Protein Tech, 66009-1-Ig), anti-CHGB (Abcam, ab12242) or anti-VGF (Abcam, ab69989).

    Techniques: CRISPR, Immunofluorescence, Western Blot, Migration, High Molecular Weight, Clone Assay