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  • 94
    Vector Laboratories n acetylgalactosamine
    N Acetylgalactosamine, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/n acetylgalactosamine/product/Vector Laboratories
    Average 94 stars, based on 20 article reviews
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    95
    Millipore udp galnac
    A distribution of products and intermediates are formed in the PglH reaction. PglH reactions were prepared with 28 μM <t>UDP-GalNAc</t> and 4 μM Und-PP-Bac2,4diNAc-(GalNAc) 2 ( H 0 ) and aliquots were extracted at the given time points then analyzed by NP-HPLC. a) The quantity of each intermediate was calculated based on their distribution as analyzed by NP-HPLC and the total counts in the reaction. Product concentration is provided at the indicated time points for total (closed circles), H 1 (open diamond), H 2 (closed squares) and H 3 (open triangle). b) The percentage of the total product was calculated for each time point and plotted H 1 (open diamond), H 2 (closed squares) and H 3 (open triangle). Note that H 2 stays at the same percentage throughout the reaction and that H 1 and H 2 levels sharply increase initially, but then stabilize as H 3 is the major product. Also, note that the lines are drawn for illustrative purposes only.
    Udp Galnac, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 167 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore n acetylgalactosamine galnac
    A distribution of products and intermediates are formed in the PglH reaction. PglH reactions were prepared with 28 μM <t>UDP-GalNAc</t> and 4 μM Und-PP-Bac2,4diNAc-(GalNAc) 2 ( H 0 ) and aliquots were extracted at the given time points then analyzed by NP-HPLC. a) The quantity of each intermediate was calculated based on their distribution as analyzed by NP-HPLC and the total counts in the reaction. Product concentration is provided at the indicated time points for total (closed circles), H 1 (open diamond), H 2 (closed squares) and H 3 (open triangle). b) The percentage of the total product was calculated for each time point and plotted H 1 (open diamond), H 2 (closed squares) and H 3 (open triangle). Note that H 2 stays at the same percentage throughout the reaction and that H 1 and H 2 levels sharply increase initially, but then stabilize as H 3 is the major product. Also, note that the lines are drawn for illustrative purposes only.
    N Acetylgalactosamine Galnac, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Seikagaku n acetylgalactosamine galnac
    HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N <t>-acetylgalactosamine;</t> Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.
    N Acetylgalactosamine Galnac, supplied by Seikagaku, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Toronto Research Chemicals n acetylgalactosamine galnac
    HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N <t>-acetylgalactosamine;</t> Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.
    N Acetylgalactosamine Galnac, supplied by Toronto Research Chemicals, used in various techniques. Bioz Stars score: 88/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Fisher Scientific n acetylgalactosamine galnac
    HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N <t>-acetylgalactosamine;</t> Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.
    N Acetylgalactosamine Galnac, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 3 article reviews
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    88
    Fuji Pharma n acetylgalactosamine galnac
    HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N <t>-acetylgalactosamine;</t> Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.
    N Acetylgalactosamine Galnac, supplied by Fuji Pharma, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Research Products International n acetylgalactosamine
    HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N <t>-acetylgalactosamine;</t> Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.
    N Acetylgalactosamine, supplied by Research Products International, used in various techniques. Bioz Stars score: 89/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/n acetylgalactosamine/product/Research Products International
    Average 89 stars, based on 3 article reviews
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    89
    Santa Cruz Biotechnology n acetylgalactosamine
    HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N <t>-acetylgalactosamine;</t> Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.
    N Acetylgalactosamine, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 89 stars, based on 19 article reviews
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    90
    Regulus Therapeutics n acetylgalactosamine
    HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N <t>-acetylgalactosamine;</t> Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.
    N Acetylgalactosamine, supplied by Regulus Therapeutics, used in various techniques. Bioz Stars score: 90/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore galnac
    Loss of SSPN impairs utrophin expression and glycosylation of α-DG. (A) Skeletal muscle lysates from wild-type (WT) and SSPN-deficient (SSPN −/− ) mice were enriched by <t>sWGA</t> lectin chromatography, and 10-µg protein samples were immunoblotted with the indicated antibodies. (B) Skeletal muscle protein lysates from WT muscle and SSPN-null (SSPN −/− ) mice were enriched by WFA lectin affinity chromatography, and nitrocellulose transfers of 10-µg WFA eluates were probed with the indicated antibodies or incubated with WFA lectin (WFA). Immunoblot exposures for each antibody/lectin staining are identical in Fig. 6 F , permitting direct comparisons. (C) sWGA-enriched protein samples were separated by ultracentrifugation through 5–20% sucrose gradients. Fraction numbers are indicated above the panels, where fraction 1 represents the lightest region of the gradient. Protein samples were analyzed by immunoblotting to the indicated antibodies, and exposures are identical for WT and SSPN-null fractions. (D) Quantitative RT-PCR was used to investigate whether loss of SSPN alters RNA levels of CT <t>GalNAc</t> transferase ( Galgt2 ). Data are expressed relative to that of WT controls. Error bars represent standard deviation ( n = 4 mice per genotype). (E) Skeletal muscle from WT and SSPN-deficient (SSPN −/− ) muscles were solubilized in 60 µg RIPA buffer and analyzed by immunoblots with Galgt2 antibodies. (F) Quantitative RT-PCR was used to investigate the effect of SSPN on utrophin (Utr) mRNA levels. RNA was isolated from WT, SSPN-null (SSPN −/− ), LARGE-null ( myd ), SSPN-deficient myd ( myd :SSPN −/− ), and threefold SSPN-Tg: myd ( myd 3.0 ) skeletal muscle. mRNA expression levels were normalized to GAPDH mRNA. Data are expressed relative to that of WT controls. Error bars represent standard deviation ( n = 3 mice per genotype; ***, P
    Galnac, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 213 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 213 article reviews
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    84
    Alnylam galnac n acetylgalactosamine sirna conjugates
    <t>siRNA</t> delivery platforms that have been evaluated preclinically and clinically. Varieties of lipids or lipidoids, siRNA conjugates, peptides, polymers, exosomes, dendrimers, etc. have been explored and employed for siRNA therapeutic development by biotech companies or institutes. The chemical structures of the key component(s) of the discussed delivery platforms, including Dlin-DMA, Dlin-MC3-DMA, C12-200, cKK-E12, GalNAc–siRNA conjugates, MLP-based DPC2.0 (EX-1), PNP, PEI, PLGA-based LODER, PTMS, GDDC4, PAsp(DET), cyclodextrin-based RONDEL™ and dendrimer generation 3 are shown. DLin-DMA (1,2-dilinoleyloxy-3-dimethylaminopropane), DLin-MC3-DMA (6Z,9Z,28Z,31Z)-heptatriaconta-6,9,28,31-tetraen-19-yl-4-(dimethylamino) butanoate, DPC Dynamic PolyConjugates, MLP membrane-lytic peptide, CDM carboxylated dimethyl maleic acid, PEG polyethylene glycol, NAG N <t>-acetylgalactosamine,</t> PNP polypeptide nanoparticle, PEI poly(ethyleneimine), LODER LOcal Drug EluteR, PLGA poly(lactic-co-glycolic) acid, PTMS PEG-PTTMA-P(GMA-S-DMA) poly(ethylene glycol)-co-poly[(2,4,6-trimethoxybenzylidene-1,1,1-tris(hydroxymethyl))] ethane methacrylate-co-poly(dimethylamino glycidyl methacrylate), GDDC4 PG-P(DPAx-co-DMAEMAy)-PCB, where PG is guanidinated poly(aminoethyl methacrylate) PCB is poly(carboxybetaine) and P(DPAx-co-DMAEMAy) is poly(dimethylaminoethyl methacrylate-co-diisopropylethyl methacrylate), PEG-PAsp(DET) polyethylene glycol-b-poly( N ′-( N -(2-aminoethyl)-2-aminoethyl) aspartamide), PBAVE polymer composed of butyl and amino vinyl ether, RONDEL™ RNAi/oligonucleotide nanoparticle delivery
    Galnac N Acetylgalactosamine Sirna Conjugates, supplied by Alnylam, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Regulus Therapeutics n acetylgalactosamine galnac conjugated anti mir 103 107
    <t>siRNA</t> delivery platforms that have been evaluated preclinically and clinically. Varieties of lipids or lipidoids, siRNA conjugates, peptides, polymers, exosomes, dendrimers, etc. have been explored and employed for siRNA therapeutic development by biotech companies or institutes. The chemical structures of the key component(s) of the discussed delivery platforms, including Dlin-DMA, Dlin-MC3-DMA, C12-200, cKK-E12, GalNAc–siRNA conjugates, MLP-based DPC2.0 (EX-1), PNP, PEI, PLGA-based LODER, PTMS, GDDC4, PAsp(DET), cyclodextrin-based RONDEL™ and dendrimer generation 3 are shown. DLin-DMA (1,2-dilinoleyloxy-3-dimethylaminopropane), DLin-MC3-DMA (6Z,9Z,28Z,31Z)-heptatriaconta-6,9,28,31-tetraen-19-yl-4-(dimethylamino) butanoate, DPC Dynamic PolyConjugates, MLP membrane-lytic peptide, CDM carboxylated dimethyl maleic acid, PEG polyethylene glycol, NAG N <t>-acetylgalactosamine,</t> PNP polypeptide nanoparticle, PEI poly(ethyleneimine), LODER LOcal Drug EluteR, PLGA poly(lactic-co-glycolic) acid, PTMS PEG-PTTMA-P(GMA-S-DMA) poly(ethylene glycol)-co-poly[(2,4,6-trimethoxybenzylidene-1,1,1-tris(hydroxymethyl))] ethane methacrylate-co-poly(dimethylamino glycidyl methacrylate), GDDC4 PG-P(DPAx-co-DMAEMAy)-PCB, where PG is guanidinated poly(aminoethyl methacrylate) PCB is poly(carboxybetaine) and P(DPAx-co-DMAEMAy) is poly(dimethylaminoethyl methacrylate-co-diisopropylethyl methacrylate), PEG-PAsp(DET) polyethylene glycol-b-poly( N ′-( N -(2-aminoethyl)-2-aminoethyl) aspartamide), PBAVE polymer composed of butyl and amino vinyl ether, RONDEL™ RNAi/oligonucleotide nanoparticle delivery
    N Acetylgalactosamine Galnac Conjugated Anti Mir 103 107, supplied by Regulus Therapeutics, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/n acetylgalactosamine galnac conjugated anti mir 103 107/product/Regulus Therapeutics
    Average 92 stars, based on 10 article reviews
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    93
    Glycon Biochemicals galnac
    Steric conflict in the formation of the transglycosylation product with the β(1-3) glycosidic bond. ( A ). Overlay of docked orientations of <t>GlcNAc</t> ( blue ) and <t>GalNAc</t> ( yellow ) acceptors with C-3 or C-4 (GlcNAc in magenta ) close to Glu371 in the WT-GlcNAcox complex. Active site residues within 3 Å from the GalNAc N -acetyl group are shown. ( A ) change that would be required in the C-3 position for product formation is indicated by the red dotted arrow. ( B ) Expected orientation of the GalNAc acceptor needed for the formation of GalNAc-β(1-3)-GlcNAc in the active site of WT-GlcNAcox. Position of the acceptor is determined from the alignment with N , N ′-diacetylchitobiose (PDB ID: 1qbb). Intersection of the molecular surfaces of GalNAc ( yellow ) and Trp444 ( cyan ) shows that the GalNAc acceptor cannot move closer to the transglycosylation donor for the product formation due to steric hindrance.
    Galnac, supplied by Glycon Biochemicals, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 2 article reviews
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    93
    Carbosynth galnac
    Steric conflict in the formation of the transglycosylation product with the β(1-3) glycosidic bond. ( A ). Overlay of docked orientations of <t>GlcNAc</t> ( blue ) and <t>GalNAc</t> ( yellow ) acceptors with C-3 or C-4 (GlcNAc in magenta ) close to Glu371 in the WT-GlcNAcox complex. Active site residues within 3 Å from the GalNAc N -acetyl group are shown. ( A ) change that would be required in the C-3 position for product formation is indicated by the red dotted arrow. ( B ) Expected orientation of the GalNAc acceptor needed for the formation of GalNAc-β(1-3)-GlcNAc in the active site of WT-GlcNAcox. Position of the acceptor is determined from the alignment with N , N ′-diacetylchitobiose (PDB ID: 1qbb). Intersection of the molecular surfaces of GalNAc ( yellow ) and Trp444 ( cyan ) shows that the GalNAc acceptor cannot move closer to the transglycosylation donor for the product formation due to steric hindrance.
    Galnac, supplied by Carbosynth, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    PerkinElmer n acetylgalactosamine
    Steric conflict in the formation of the transglycosylation product with the β(1-3) glycosidic bond. ( A ). Overlay of docked orientations of <t>GlcNAc</t> ( blue ) and <t>GalNAc</t> ( yellow ) acceptors with C-3 or C-4 (GlcNAc in magenta ) close to Glu371 in the WT-GlcNAcox complex. Active site residues within 3 Å from the GalNAc N -acetyl group are shown. ( A ) change that would be required in the C-3 position for product formation is indicated by the red dotted arrow. ( B ) Expected orientation of the GalNAc acceptor needed for the formation of GalNAc-β(1-3)-GlcNAc in the active site of WT-GlcNAcox. Position of the acceptor is determined from the alignment with N , N ′-diacetylchitobiose (PDB ID: 1qbb). Intersection of the molecular surfaces of GalNAc ( yellow ) and Trp444 ( cyan ) shows that the GalNAc acceptor cannot move closer to the transglycosylation donor for the product formation due to steric hindrance.
    N Acetylgalactosamine, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 89/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    GE Healthcare n acetylgalactosamine
    Steric conflict in the formation of the transglycosylation product with the β(1-3) glycosidic bond. ( A ). Overlay of docked orientations of <t>GlcNAc</t> ( blue ) and <t>GalNAc</t> ( yellow ) acceptors with C-3 or C-4 (GlcNAc in magenta ) close to Glu371 in the WT-GlcNAcox complex. Active site residues within 3 Å from the GalNAc N -acetyl group are shown. ( A ) change that would be required in the C-3 position for product formation is indicated by the red dotted arrow. ( B ) Expected orientation of the GalNAc acceptor needed for the formation of GalNAc-β(1-3)-GlcNAc in the active site of WT-GlcNAcox. Position of the acceptor is determined from the alignment with N , N ′-diacetylchitobiose (PDB ID: 1qbb). Intersection of the molecular surfaces of GalNAc ( yellow ) and Trp444 ( cyan ) shows that the GalNAc acceptor cannot move closer to the transglycosylation donor for the product formation due to steric hindrance.
    N Acetylgalactosamine, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 89/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Applichem galnac
    Vicia villosa chromatographic profiles from fallow deer. Fractions were issued from fetal cotyledonary (A) and maternal caruncula (B) tissues. The column (2.3 × 2 cm; 8 ml) was previously equilibrated with 0.01 M <t>HEPES</t> buffer (pH 7.6). The elution with 0.15 M NaCl or 0.05 M <t>GalNAc</t> buffer (containing 0.15 M NaCl) were designated by arrow. The pooled fractions are in gray.
    Galnac, supplied by Applichem, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore m galnac
    Vicia villosa chromatographic profiles from fallow deer. Fractions were issued from fetal cotyledonary (A) and maternal caruncula (B) tissues. The column (2.3 × 2 cm; 8 ml) was previously equilibrated with 0.01 M <t>HEPES</t> buffer (pH 7.6). The elution with 0.15 M NaCl or 0.05 M <t>GalNAc</t> buffer (containing 0.15 M NaCl) were designated by arrow. The pooled fractions are in gray.
    M Galnac, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    A distribution of products and intermediates are formed in the PglH reaction. PglH reactions were prepared with 28 μM UDP-GalNAc and 4 μM Und-PP-Bac2,4diNAc-(GalNAc) 2 ( H 0 ) and aliquots were extracted at the given time points then analyzed by NP-HPLC. a) The quantity of each intermediate was calculated based on their distribution as analyzed by NP-HPLC and the total counts in the reaction. Product concentration is provided at the indicated time points for total (closed circles), H 1 (open diamond), H 2 (closed squares) and H 3 (open triangle). b) The percentage of the total product was calculated for each time point and plotted H 1 (open diamond), H 2 (closed squares) and H 3 (open triangle). Note that H 2 stays at the same percentage throughout the reaction and that H 1 and H 2 levels sharply increase initially, but then stabilize as H 3 is the major product. Also, note that the lines are drawn for illustrative purposes only.

    Journal: Biochemistry

    Article Title: Campylobacter Jejuni PglH is a Single Active Site Processive Polymerase that Utilizes Product Inhibition to Limit Sequential Glycosyl Transfer Reactions

    doi: 10.1021/bi802284d

    Figure Lengend Snippet: A distribution of products and intermediates are formed in the PglH reaction. PglH reactions were prepared with 28 μM UDP-GalNAc and 4 μM Und-PP-Bac2,4diNAc-(GalNAc) 2 ( H 0 ) and aliquots were extracted at the given time points then analyzed by NP-HPLC. a) The quantity of each intermediate was calculated based on their distribution as analyzed by NP-HPLC and the total counts in the reaction. Product concentration is provided at the indicated time points for total (closed circles), H 1 (open diamond), H 2 (closed squares) and H 3 (open triangle). b) The percentage of the total product was calculated for each time point and plotted H 1 (open diamond), H 2 (closed squares) and H 3 (open triangle). Note that H 2 stays at the same percentage throughout the reaction and that H 1 and H 2 levels sharply increase initially, but then stabilize as H 3 is the major product. Also, note that the lines are drawn for illustrative purposes only.

    Article Snippet: The UDP-N,N′-diacetylbacillosamine was prepared as previously described ( ) and the UDP-GalNAc was purchased from Sigma–Aldrich.

    Techniques: Normal Phase Liquid Chromatography, Concentration Assay

    PglH utilizes the highly conserved EX 7 E motif flanked by residues E265 and E273 for catalysis of all reactions. Reactions containing the indicated PglH mutants (20 nM) were prepared and the amount of product determined for an overnight reaction with H 0 (68 nM) and UDP-[ 3 H]GalNAc (20 Ci/mmol; 250 nM).

    Journal: Biochemistry

    Article Title: Campylobacter Jejuni PglH is a Single Active Site Processive Polymerase that Utilizes Product Inhibition to Limit Sequential Glycosyl Transfer Reactions

    doi: 10.1021/bi802284d

    Figure Lengend Snippet: PglH utilizes the highly conserved EX 7 E motif flanked by residues E265 and E273 for catalysis of all reactions. Reactions containing the indicated PglH mutants (20 nM) were prepared and the amount of product determined for an overnight reaction with H 0 (68 nM) and UDP-[ 3 H]GalNAc (20 Ci/mmol; 250 nM).

    Article Snippet: The UDP-N,N′-diacetylbacillosamine was prepared as previously described ( ) and the UDP-GalNAc was purchased from Sigma–Aldrich.

    Techniques:

    The concentration of substrate determines the distribution of products and intermediates in a PglH reaction. PglH reactions were prepared with either a) 4.3 μM Und-PP-Bac2,4diNAc-[ 3 H]GalNAc-GalNAc ( H 0 ) and 0.25 μM UDP-[ 3 H]GalNAc or b) 0.26 μM Und-PP-Bac2,4diNAc-[ 3 H]GalNAc-GalNAc ( H 0 ) and 0.25 μM UDP-[ 3 H]GalNAc. Each column represents the amount of radioactivity in a 1 mL fraction at the corresponding time corrected for the number of [ 3 H]GalNAc units incorporated into each. Note that with high polyisoprene-linked substrate relative to UDP-[ 3 H]GalNAc the majority of the product is the first intermediate ( H 1 ), and when the substrates are approximately equimolar the major product is the final product ( H 3 ). The identity of H 1 and H 2 were based on consistent normal phase HPLC retention times of the tritium-labeled PglH products and quantitative conversion of the isolated intermediate to H 3 upon further incubation with PglH.

    Journal: Biochemistry

    Article Title: Campylobacter Jejuni PglH is a Single Active Site Processive Polymerase that Utilizes Product Inhibition to Limit Sequential Glycosyl Transfer Reactions

    doi: 10.1021/bi802284d

    Figure Lengend Snippet: The concentration of substrate determines the distribution of products and intermediates in a PglH reaction. PglH reactions were prepared with either a) 4.3 μM Und-PP-Bac2,4diNAc-[ 3 H]GalNAc-GalNAc ( H 0 ) and 0.25 μM UDP-[ 3 H]GalNAc or b) 0.26 μM Und-PP-Bac2,4diNAc-[ 3 H]GalNAc-GalNAc ( H 0 ) and 0.25 μM UDP-[ 3 H]GalNAc. Each column represents the amount of radioactivity in a 1 mL fraction at the corresponding time corrected for the number of [ 3 H]GalNAc units incorporated into each. Note that with high polyisoprene-linked substrate relative to UDP-[ 3 H]GalNAc the majority of the product is the first intermediate ( H 1 ), and when the substrates are approximately equimolar the major product is the final product ( H 3 ). The identity of H 1 and H 2 were based on consistent normal phase HPLC retention times of the tritium-labeled PglH products and quantitative conversion of the isolated intermediate to H 3 upon further incubation with PglH.

    Article Snippet: The UDP-N,N′-diacetylbacillosamine was prepared as previously described ( ) and the UDP-GalNAc was purchased from Sigma–Aldrich.

    Techniques: Concentration Assay, Radioactivity, High Performance Liquid Chromatography, Labeling, Isolation, Incubation

    K m values for UDP- N -acetylgalactosamine and pNP-GlcNAc

    Journal: The Journal of biological chemistry

    Article Title: Molecular Cloning and Functional Characterization of a Lepidopteran Insect β4-N-Acetylgalactosaminyltransferase with Broad Substrate Specificity, a Functional Role in Glycoprotein Biosynthesis, and a Potential Functional Role in Glycolipid Biosynthesis

    doi: 10.1074/jbc.M404925200

    Figure Lengend Snippet: K m values for UDP- N -acetylgalactosamine and pNP-GlcNAc

    Article Snippet: To determine the apparent Km for the donor substrate, assays were performed in the presence of 1.0 m m pNP-GlcNAc, nonradioactive UDP- N -acetylgalactosamine (Sigma) concentrations ranging from 0.150 to 12 m m , and a constant ratio of tritiated UDP- N -acetylgalactosamine with a specific activity of 15 Ci/mmol.

    Techniques:

    HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N -acetylgalactosamine; Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.

    Journal: Biomolecules

    Article Title: Development and Application of Multidimensional HPLC Mapping Method for O-linked Oligosaccharides

    doi: 10.3390/biom1010048

    Figure Lengend Snippet: HPLC map of O -glycans. •, neutral; ▪, sialylated; ♦, sulfated glycans. Key: Gal, galactose; Glc, Glucose; GlcNAc, N -acetylglucosamine; GalN, N -acetylgalactosamine; Man, mannose; Fuc, fucose; S, sulfate; Neu, N -acetylneuraminic acid.

    Article Snippet: 2-Aminopyridine-derivatized (PA) isomalto-oligosaccharides were prepared from glucose oligomers (1-20) (Seikagaku Kogyo Co., Tokyo, Japan), fucose (Fuc), galactose (Gal), N -acetylgalactosamine (GalNAc) (Seikagaku Kogyo Co., Tokyo, Japan), glucose (Glc), N -acetylglucosamine (GlcNAc), mannose (Man), Galβ1-3GalNAc (Calbiochem, Schwalbach, Germany), and Galβ1-3(Fucα1-2)GalNAc.

    Techniques: High Performance Liquid Chromatography, Gas Chromatography

    Loss of SSPN impairs utrophin expression and glycosylation of α-DG. (A) Skeletal muscle lysates from wild-type (WT) and SSPN-deficient (SSPN −/− ) mice were enriched by sWGA lectin chromatography, and 10-µg protein samples were immunoblotted with the indicated antibodies. (B) Skeletal muscle protein lysates from WT muscle and SSPN-null (SSPN −/− ) mice were enriched by WFA lectin affinity chromatography, and nitrocellulose transfers of 10-µg WFA eluates were probed with the indicated antibodies or incubated with WFA lectin (WFA). Immunoblot exposures for each antibody/lectin staining are identical in Fig. 6 F , permitting direct comparisons. (C) sWGA-enriched protein samples were separated by ultracentrifugation through 5–20% sucrose gradients. Fraction numbers are indicated above the panels, where fraction 1 represents the lightest region of the gradient. Protein samples were analyzed by immunoblotting to the indicated antibodies, and exposures are identical for WT and SSPN-null fractions. (D) Quantitative RT-PCR was used to investigate whether loss of SSPN alters RNA levels of CT GalNAc transferase ( Galgt2 ). Data are expressed relative to that of WT controls. Error bars represent standard deviation ( n = 4 mice per genotype). (E) Skeletal muscle from WT and SSPN-deficient (SSPN −/− ) muscles were solubilized in 60 µg RIPA buffer and analyzed by immunoblots with Galgt2 antibodies. (F) Quantitative RT-PCR was used to investigate the effect of SSPN on utrophin (Utr) mRNA levels. RNA was isolated from WT, SSPN-null (SSPN −/− ), LARGE-null ( myd ), SSPN-deficient myd ( myd :SSPN −/− ), and threefold SSPN-Tg: myd ( myd 3.0 ) skeletal muscle. mRNA expression levels were normalized to GAPDH mRNA. Data are expressed relative to that of WT controls. Error bars represent standard deviation ( n = 3 mice per genotype; ***, P

    Journal: The Journal of Cell Biology

    Article Title: Sarcospan-dependent Akt activation is required for utrophin expression and muscle regeneration

    doi: 10.1083/jcb.201110032

    Figure Lengend Snippet: Loss of SSPN impairs utrophin expression and glycosylation of α-DG. (A) Skeletal muscle lysates from wild-type (WT) and SSPN-deficient (SSPN −/− ) mice were enriched by sWGA lectin chromatography, and 10-µg protein samples were immunoblotted with the indicated antibodies. (B) Skeletal muscle protein lysates from WT muscle and SSPN-null (SSPN −/− ) mice were enriched by WFA lectin affinity chromatography, and nitrocellulose transfers of 10-µg WFA eluates were probed with the indicated antibodies or incubated with WFA lectin (WFA). Immunoblot exposures for each antibody/lectin staining are identical in Fig. 6 F , permitting direct comparisons. (C) sWGA-enriched protein samples were separated by ultracentrifugation through 5–20% sucrose gradients. Fraction numbers are indicated above the panels, where fraction 1 represents the lightest region of the gradient. Protein samples were analyzed by immunoblotting to the indicated antibodies, and exposures are identical for WT and SSPN-null fractions. (D) Quantitative RT-PCR was used to investigate whether loss of SSPN alters RNA levels of CT GalNAc transferase ( Galgt2 ). Data are expressed relative to that of WT controls. Error bars represent standard deviation ( n = 4 mice per genotype). (E) Skeletal muscle from WT and SSPN-deficient (SSPN −/− ) muscles were solubilized in 60 µg RIPA buffer and analyzed by immunoblots with Galgt2 antibodies. (F) Quantitative RT-PCR was used to investigate the effect of SSPN on utrophin (Utr) mRNA levels. RNA was isolated from WT, SSPN-null (SSPN −/− ), LARGE-null ( myd ), SSPN-deficient myd ( myd :SSPN −/− ), and threefold SSPN-Tg: myd ( myd 3.0 ) skeletal muscle. mRNA expression levels were normalized to GAPDH mRNA. Data are expressed relative to that of WT controls. Error bars represent standard deviation ( n = 3 mice per genotype; ***, P

    Article Snippet: Bound proteins were eluted with 0.3 M GlcNAc (sWGA) or 0.3 M GalNAc (WFA; Sigma-Aldrich) and concentrated using filtration columns (Centricon Ultracel; Millipore) by centrifugation at 4,000 g for 20 min.

    Techniques: Expressing, Mouse Assay, Chromatography, Affinity Chromatography, Incubation, Staining, Quantitative RT-PCR, Standard Deviation, Western Blot, Isolation

    SSPN increases cell surface glycosylation in mdx muscle. (A and B) Transverse cryosections of quadriceps muscles from SSPN-Tg (A) or Akt transgenic (B) muscles were stained with biotinylated Wisteria floribunda agglutinin (WFA) and visualized by indirect immunofluorescence. Bars, 50 µm. (C) Skeletal muscle protein lysates from the indicated mouse models were enriched by WFA lectin affinity chromatography (WFA enrichment) and analyzed with indicated antibodies and overlayed (O/L) with WFA lectin (WFA O/L). (D) Skeletal muscle protein lysates were enriched by WFA lectin affinity chromatography (WFA enrichment) and subjected to the same analysis as described in C. (E) WFA and laminin overlay assays were performed on protein lysates enriched with succinylated WGA (sWGA) lectin chromatography from mdx and Akt transgenic mdx ( mdx Akt ) muscle. Mice were treated with doxycycline to induce Akt expression in skeletal muscle as described previously ( Peter et al., 2009 ). Laminin overlays (Lam O/L) represent binding to immobilized α-DG on nitrocellulose transfers. Immunoblotting with antibodies to α-DG is shown. (F) Levels of WFA binding to α-DG were quantitated by densitometry of bands from overlay assays, and data are expressed relative to mdx levels (100%). Error bars represent standard deviation of the mean ( n = 2–3 muscle preps per genotype). (G) Quantitative RT-PCR was used to investigate whether overexpression of SSPN alters RNA levels of CT GalNAc transferase ( Galgt2 ). RNA was isolated from WT, WT 1.5 , mdx , and mdx 1.5 skeletal muscle. Data are expressed relative to non-Tg WT controls. Error bars represent standard error of the mean (*, P

    Journal: The Journal of Cell Biology

    Article Title: Sarcospan-dependent Akt activation is required for utrophin expression and muscle regeneration

    doi: 10.1083/jcb.201110032

    Figure Lengend Snippet: SSPN increases cell surface glycosylation in mdx muscle. (A and B) Transverse cryosections of quadriceps muscles from SSPN-Tg (A) or Akt transgenic (B) muscles were stained with biotinylated Wisteria floribunda agglutinin (WFA) and visualized by indirect immunofluorescence. Bars, 50 µm. (C) Skeletal muscle protein lysates from the indicated mouse models were enriched by WFA lectin affinity chromatography (WFA enrichment) and analyzed with indicated antibodies and overlayed (O/L) with WFA lectin (WFA O/L). (D) Skeletal muscle protein lysates were enriched by WFA lectin affinity chromatography (WFA enrichment) and subjected to the same analysis as described in C. (E) WFA and laminin overlay assays were performed on protein lysates enriched with succinylated WGA (sWGA) lectin chromatography from mdx and Akt transgenic mdx ( mdx Akt ) muscle. Mice were treated with doxycycline to induce Akt expression in skeletal muscle as described previously ( Peter et al., 2009 ). Laminin overlays (Lam O/L) represent binding to immobilized α-DG on nitrocellulose transfers. Immunoblotting with antibodies to α-DG is shown. (F) Levels of WFA binding to α-DG were quantitated by densitometry of bands from overlay assays, and data are expressed relative to mdx levels (100%). Error bars represent standard deviation of the mean ( n = 2–3 muscle preps per genotype). (G) Quantitative RT-PCR was used to investigate whether overexpression of SSPN alters RNA levels of CT GalNAc transferase ( Galgt2 ). RNA was isolated from WT, WT 1.5 , mdx , and mdx 1.5 skeletal muscle. Data are expressed relative to non-Tg WT controls. Error bars represent standard error of the mean (*, P

    Article Snippet: Bound proteins were eluted with 0.3 M GlcNAc (sWGA) or 0.3 M GalNAc (WFA; Sigma-Aldrich) and concentrated using filtration columns (Centricon Ultracel; Millipore) by centrifugation at 4,000 g for 20 min.

    Techniques: Transgenic Assay, Staining, Immunofluorescence, Affinity Chromatography, Whole Genome Amplification, Chromatography, Mouse Assay, Expressing, Laser Capture Microdissection, Binding Assay, Standard Deviation, Quantitative RT-PCR, Over Expression, Isolation

    siRNA delivery platforms that have been evaluated preclinically and clinically. Varieties of lipids or lipidoids, siRNA conjugates, peptides, polymers, exosomes, dendrimers, etc. have been explored and employed for siRNA therapeutic development by biotech companies or institutes. The chemical structures of the key component(s) of the discussed delivery platforms, including Dlin-DMA, Dlin-MC3-DMA, C12-200, cKK-E12, GalNAc–siRNA conjugates, MLP-based DPC2.0 (EX-1), PNP, PEI, PLGA-based LODER, PTMS, GDDC4, PAsp(DET), cyclodextrin-based RONDEL™ and dendrimer generation 3 are shown. DLin-DMA (1,2-dilinoleyloxy-3-dimethylaminopropane), DLin-MC3-DMA (6Z,9Z,28Z,31Z)-heptatriaconta-6,9,28,31-tetraen-19-yl-4-(dimethylamino) butanoate, DPC Dynamic PolyConjugates, MLP membrane-lytic peptide, CDM carboxylated dimethyl maleic acid, PEG polyethylene glycol, NAG N -acetylgalactosamine, PNP polypeptide nanoparticle, PEI poly(ethyleneimine), LODER LOcal Drug EluteR, PLGA poly(lactic-co-glycolic) acid, PTMS PEG-PTTMA-P(GMA-S-DMA) poly(ethylene glycol)-co-poly[(2,4,6-trimethoxybenzylidene-1,1,1-tris(hydroxymethyl))] ethane methacrylate-co-poly(dimethylamino glycidyl methacrylate), GDDC4 PG-P(DPAx-co-DMAEMAy)-PCB, where PG is guanidinated poly(aminoethyl methacrylate) PCB is poly(carboxybetaine) and P(DPAx-co-DMAEMAy) is poly(dimethylaminoethyl methacrylate-co-diisopropylethyl methacrylate), PEG-PAsp(DET) polyethylene glycol-b-poly( N ′-( N -(2-aminoethyl)-2-aminoethyl) aspartamide), PBAVE polymer composed of butyl and amino vinyl ether, RONDEL™ RNAi/oligonucleotide nanoparticle delivery

    Journal: Signal Transduction and Targeted Therapy

    Article Title: Therapeutic siRNA: state of the art

    doi: 10.1038/s41392-020-0207-x

    Figure Lengend Snippet: siRNA delivery platforms that have been evaluated preclinically and clinically. Varieties of lipids or lipidoids, siRNA conjugates, peptides, polymers, exosomes, dendrimers, etc. have been explored and employed for siRNA therapeutic development by biotech companies or institutes. The chemical structures of the key component(s) of the discussed delivery platforms, including Dlin-DMA, Dlin-MC3-DMA, C12-200, cKK-E12, GalNAc–siRNA conjugates, MLP-based DPC2.0 (EX-1), PNP, PEI, PLGA-based LODER, PTMS, GDDC4, PAsp(DET), cyclodextrin-based RONDEL™ and dendrimer generation 3 are shown. DLin-DMA (1,2-dilinoleyloxy-3-dimethylaminopropane), DLin-MC3-DMA (6Z,9Z,28Z,31Z)-heptatriaconta-6,9,28,31-tetraen-19-yl-4-(dimethylamino) butanoate, DPC Dynamic PolyConjugates, MLP membrane-lytic peptide, CDM carboxylated dimethyl maleic acid, PEG polyethylene glycol, NAG N -acetylgalactosamine, PNP polypeptide nanoparticle, PEI poly(ethyleneimine), LODER LOcal Drug EluteR, PLGA poly(lactic-co-glycolic) acid, PTMS PEG-PTTMA-P(GMA-S-DMA) poly(ethylene glycol)-co-poly[(2,4,6-trimethoxybenzylidene-1,1,1-tris(hydroxymethyl))] ethane methacrylate-co-poly(dimethylamino glycidyl methacrylate), GDDC4 PG-P(DPAx-co-DMAEMAy)-PCB, where PG is guanidinated poly(aminoethyl methacrylate) PCB is poly(carboxybetaine) and P(DPAx-co-DMAEMAy) is poly(dimethylaminoethyl methacrylate-co-diisopropylethyl methacrylate), PEG-PAsp(DET) polyethylene glycol-b-poly( N ′-( N -(2-aminoethyl)-2-aminoethyl) aspartamide), PBAVE polymer composed of butyl and amino vinyl ether, RONDEL™ RNAi/oligonucleotide nanoparticle delivery

    Article Snippet: Furthermore, investigators from Alnylam have disclosed that the hepatotoxicity of GalNAc (N -acetylgalactosamine)-siRNA conjugates is attributed to off-target gene silencing mediated by miRNA-like recognition between siRNA and a mistargeted RNA.

    Techniques:

    Steric conflict in the formation of the transglycosylation product with the β(1-3) glycosidic bond. ( A ). Overlay of docked orientations of GlcNAc ( blue ) and GalNAc ( yellow ) acceptors with C-3 or C-4 (GlcNAc in magenta ) close to Glu371 in the WT-GlcNAcox complex. Active site residues within 3 Å from the GalNAc N -acetyl group are shown. ( A ) change that would be required in the C-3 position for product formation is indicated by the red dotted arrow. ( B ) Expected orientation of the GalNAc acceptor needed for the formation of GalNAc-β(1-3)-GlcNAc in the active site of WT-GlcNAcox. Position of the acceptor is determined from the alignment with N , N ′-diacetylchitobiose (PDB ID: 1qbb). Intersection of the molecular surfaces of GalNAc ( yellow ) and Trp444 ( cyan ) shows that the GalNAc acceptor cannot move closer to the transglycosylation donor for the product formation due to steric hindrance.

    Journal: International Journal of Molecular Sciences

    Article Title: Acceptor Specificity of β-N-Acetylhexosaminidase from Talaromyces flavus: A Rational Explanation

    doi: 10.3390/ijms20246181

    Figure Lengend Snippet: Steric conflict in the formation of the transglycosylation product with the β(1-3) glycosidic bond. ( A ). Overlay of docked orientations of GlcNAc ( blue ) and GalNAc ( yellow ) acceptors with C-3 or C-4 (GlcNAc in magenta ) close to Glu371 in the WT-GlcNAcox complex. Active site residues within 3 Å from the GalNAc N -acetyl group are shown. ( A ) change that would be required in the C-3 position for product formation is indicated by the red dotted arrow. ( B ) Expected orientation of the GalNAc acceptor needed for the formation of GalNAc-β(1-3)-GlcNAc in the active site of WT-GlcNAcox. Position of the acceptor is determined from the alignment with N , N ′-diacetylchitobiose (PDB ID: 1qbb). Intersection of the molecular surfaces of GalNAc ( yellow ) and Trp444 ( cyan ) shows that the GalNAc acceptor cannot move closer to the transglycosylation donor for the product formation due to steric hindrance.

    Article Snippet: General Procedures Commercial substrates, namely p NP-GlcNAc and p NP-GalNAc (Goldbio, St. Louis, CA, USA), GlcNAc (Acros Organics, Geel, Belgium), GalNAc (Glycon Biochemicals, Luckenwalde, Germany), d -glucose (Lach-ner, Neratovice, CZ), d -galactose, N -acetylmuramic acid, and d -glucuronic acid (all from Sigma-Aldrich, Munich, Germany), were employed without further purification.

    Techniques:

    Products of the glycosylation of GlcNAc ( 1 ), GalNAc ( 5 ), glucose ( 2 ), and galactose ( 6 ) catalyzed by Tf Hex WT.

    Journal: International Journal of Molecular Sciences

    Article Title: Acceptor Specificity of β-N-Acetylhexosaminidase from Talaromyces flavus: A Rational Explanation

    doi: 10.3390/ijms20246181

    Figure Lengend Snippet: Products of the glycosylation of GlcNAc ( 1 ), GalNAc ( 5 ), glucose ( 2 ), and galactose ( 6 ) catalyzed by Tf Hex WT.

    Article Snippet: General Procedures Commercial substrates, namely p NP-GlcNAc and p NP-GalNAc (Goldbio, St. Louis, CA, USA), GlcNAc (Acros Organics, Geel, Belgium), GalNAc (Glycon Biochemicals, Luckenwalde, Germany), d -glucose (Lach-ner, Neratovice, CZ), d -galactose, N -acetylmuramic acid, and d -glucuronic acid (all from Sigma-Aldrich, Munich, Germany), were employed without further purification.

    Techniques:

    Vicia villosa chromatographic profiles from fallow deer. Fractions were issued from fetal cotyledonary (A) and maternal caruncula (B) tissues. The column (2.3 × 2 cm; 8 ml) was previously equilibrated with 0.01 M HEPES buffer (pH 7.6). The elution with 0.15 M NaCl or 0.05 M GalNAc buffer (containing 0.15 M NaCl) were designated by arrow. The pooled fractions are in gray.

    Journal: Acta Veterinaria Scandinavica

    Article Title: Identification of pregnancy-associated glycoproteins and alpha-fetoprotein in fallow deer (Dama dama) placenta

    doi: 10.1186/1751-0147-56-4

    Figure Lengend Snippet: Vicia villosa chromatographic profiles from fallow deer. Fractions were issued from fetal cotyledonary (A) and maternal caruncula (B) tissues. The column (2.3 × 2 cm; 8 ml) was previously equilibrated with 0.01 M HEPES buffer (pH 7.6). The elution with 0.15 M NaCl or 0.05 M GalNAc buffer (containing 0.15 M NaCl) were designated by arrow. The pooled fractions are in gray.

    Article Snippet: Proteins were eluted by using the same buffer (0.01 M HEPES + 0.15 M NaCl) added of 0.05 M GalNAc (AppliChem, Darmstadt, Germany).

    Techniques: