4 methylumbelliferyl n acetyl α d neuraminic acid munana  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc 4 methylumbelliferyl n acetyl α d neuraminic acid munana
    4 Methylumbelliferyl N Acetyl α D Neuraminic Acid Munana, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    4 methylumbelliferyl n acetyl α d neuraminic acid munana  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc 4 methylumbelliferyl n acetyl α d neuraminic acid munana
    4 Methylumbelliferyl N Acetyl α D Neuraminic Acid Munana, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    m 520 25 critical  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc m 520 25 critical
    M 520 25 Critical, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    2 4 methylumbelliferyl a d n acetylneuraminic acid sodium salt  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc 2 4 methylumbelliferyl a d n acetylneuraminic acid sodium salt
    2 4 Methylumbelliferyl A D N Acetylneuraminic Acid Sodium Salt, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    2 4 methylumbelliferyl n acetylneuraminic acid  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc 2 4 methylumbelliferyl n acetylneuraminic acid
    Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, <t>4-MU-Neu5Ac</t> assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).
    2 4 Methylumbelliferyl N Acetylneuraminic Acid, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis"

    Article Title: Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA118.006221

    Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, 4-MU-Neu5Ac assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).
    Figure Legend Snippet: Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, 4-MU-Neu5Ac assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).

    Techniques Used: Activity Assay, Expressing, Recombinant, Plasmid Preparation, Produced

    NanH2 and NanH3 cleave 3′- and 6′-sialyllactose. A and B, preparations of NanH2 (A) or NanH3 (B) were mixed with 20 μm 3′-sialyllactose (3′ SL) or 6′-sialyllactose (6′ SL) and incubated at 37 °C for 3 h. At each time point, aliquots of the reaction mixtures were removed and analyzed by DMB-HPLC for free Neu5Ac.
    Figure Legend Snippet: NanH2 and NanH3 cleave 3′- and 6′-sialyllactose. A and B, preparations of NanH2 (A) or NanH3 (B) were mixed with 20 μm 3′-sialyllactose (3′ SL) or 6′-sialyllactose (6′ SL) and incubated at 37 °C for 3 h. At each time point, aliquots of the reaction mixtures were removed and analyzed by DMB-HPLC for free Neu5Ac.

    Techniques Used: Incubation

    NanH2 and NanH3 act on N-linked and O-linked sialoglycan substrates relevant to the host mucosa. A–D, sialoglycans included SIgA from human colostrum (A), BSM (B and C), and GBS whole cells (D). Preparations of NanH2 or NanH3 were mixed with each substrate and incubated at 37 °C for 4 h. AUS was used as a positive control. At each time point, aliquots of the reaction mixtures were removed and analyzed for Neu5Ac or N-glycolylneuraminic acid (Neu5Gc) by DMB-HPLC.
    Figure Legend Snippet: NanH2 and NanH3 act on N-linked and O-linked sialoglycan substrates relevant to the host mucosa. A–D, sialoglycans included SIgA from human colostrum (A), BSM (B and C), and GBS whole cells (D). Preparations of NanH2 or NanH3 were mixed with each substrate and incubated at 37 °C for 4 h. AUS was used as a positive control. At each time point, aliquots of the reaction mixtures were removed and analyzed for Neu5Ac or N-glycolylneuraminic acid (Neu5Gc) by DMB-HPLC.

    Techniques Used: Incubation, Positive Control

    Sialidase activity of isolated recombinant NanH proteins. A, 4-MU-Neu5Ac assay on JCP8151B NanH1 isolated from E. coli lysates. B, normalization of recombinant NanH1, NanH2, and NanH3 by SDS-PAGE and Coomassie staining. MW, molecular weight. C, end point assay showing release of sialic acids from 4-MU-Neu5Ac, BSM, colostrum SIgA, and sialyllactose in the presence of NanH1, NanH2, or NanH3. Samples were incubated at 37 °C for 2 h, and free sialic acids were measured by DMB-HPLC.
    Figure Legend Snippet: Sialidase activity of isolated recombinant NanH proteins. A, 4-MU-Neu5Ac assay on JCP8151B NanH1 isolated from E. coli lysates. B, normalization of recombinant NanH1, NanH2, and NanH3 by SDS-PAGE and Coomassie staining. MW, molecular weight. C, end point assay showing release of sialic acids from 4-MU-Neu5Ac, BSM, colostrum SIgA, and sialyllactose in the presence of NanH1, NanH2, or NanH3. Samples were incubated at 37 °C for 2 h, and free sialic acids were measured by DMB-HPLC.

    Techniques Used: Activity Assay, Isolation, Recombinant, SDS Page, Staining, Molecular Weight, End Point Assay, Incubation

    2 4 methylumbelliferyl n acetylneuraminic acid  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc 2 4 methylumbelliferyl n acetylneuraminic acid
    Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, <t>4-MU-Neu5Ac</t> assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).
    2 4 Methylumbelliferyl N Acetylneuraminic Acid, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis"

    Article Title: Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.RA118.006221

    Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, 4-MU-Neu5Ac assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).
    Figure Legend Snippet: Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, 4-MU-Neu5Ac assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).

    Techniques Used: Activity Assay, Expressing, Recombinant, Plasmid Preparation, Produced

    NanH2 and NanH3 cleave 3′- and 6′-sialyllactose. A and B, preparations of NanH2 (A) or NanH3 (B) were mixed with 20 μm 3′-sialyllactose (3′ SL) or 6′-sialyllactose (6′ SL) and incubated at 37 °C for 3 h. At each time point, aliquots of the reaction mixtures were removed and analyzed by DMB-HPLC for free Neu5Ac.
    Figure Legend Snippet: NanH2 and NanH3 cleave 3′- and 6′-sialyllactose. A and B, preparations of NanH2 (A) or NanH3 (B) were mixed with 20 μm 3′-sialyllactose (3′ SL) or 6′-sialyllactose (6′ SL) and incubated at 37 °C for 3 h. At each time point, aliquots of the reaction mixtures were removed and analyzed by DMB-HPLC for free Neu5Ac.

    Techniques Used: Incubation

    NanH2 and NanH3 act on N-linked and O-linked sialoglycan substrates relevant to the host mucosa. A–D, sialoglycans included SIgA from human colostrum (A), BSM (B and C), and GBS whole cells (D). Preparations of NanH2 or NanH3 were mixed with each substrate and incubated at 37 °C for 4 h. AUS was used as a positive control. At each time point, aliquots of the reaction mixtures were removed and analyzed for Neu5Ac or N-glycolylneuraminic acid (Neu5Gc) by DMB-HPLC.
    Figure Legend Snippet: NanH2 and NanH3 act on N-linked and O-linked sialoglycan substrates relevant to the host mucosa. A–D, sialoglycans included SIgA from human colostrum (A), BSM (B and C), and GBS whole cells (D). Preparations of NanH2 or NanH3 were mixed with each substrate and incubated at 37 °C for 4 h. AUS was used as a positive control. At each time point, aliquots of the reaction mixtures were removed and analyzed for Neu5Ac or N-glycolylneuraminic acid (Neu5Gc) by DMB-HPLC.

    Techniques Used: Incubation, Positive Control

    Sialidase activity of isolated recombinant NanH proteins. A, 4-MU-Neu5Ac assay on JCP8151B NanH1 isolated from E. coli lysates. B, normalization of recombinant NanH1, NanH2, and NanH3 by SDS-PAGE and Coomassie staining. MW, molecular weight. C, end point assay showing release of sialic acids from 4-MU-Neu5Ac, BSM, colostrum SIgA, and sialyllactose in the presence of NanH1, NanH2, or NanH3. Samples were incubated at 37 °C for 2 h, and free sialic acids were measured by DMB-HPLC.
    Figure Legend Snippet: Sialidase activity of isolated recombinant NanH proteins. A, 4-MU-Neu5Ac assay on JCP8151B NanH1 isolated from E. coli lysates. B, normalization of recombinant NanH1, NanH2, and NanH3 by SDS-PAGE and Coomassie staining. MW, molecular weight. C, end point assay showing release of sialic acids from 4-MU-Neu5Ac, BSM, colostrum SIgA, and sialyllactose in the presence of NanH1, NanH2, or NanH3. Samples were incubated at 37 °C for 2 h, and free sialic acids were measured by DMB-HPLC.

    Techniques Used: Activity Assay, Isolation, Recombinant, SDS Page, Staining, Molecular Weight, End Point Assay, Incubation

    2 4 methylumbelliferyl n acetylneuraminic acid  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc 2 4 methylumbelliferyl n acetylneuraminic acid
    2 4 Methylumbelliferyl N Acetylneuraminic Acid, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    synthetic fluorogenic substrate fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc synthetic fluorogenic substrate fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt
    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using <t>4MUSia.</t> Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Synthetic Fluorogenic Substrate Fluorogenic Sialidase Substrate 2 4 Methylumbelliferyl α D N Acetylneuraminic Acid Sodium Salt, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis"

    Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M111.278135

    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Figure Legend Snippet: Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

    Techniques Used: Activity Assay, Staining, Concentration Assay

    BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.
    Figure Legend Snippet: BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

    Techniques Used: Incubation, MANN-WHITNEY, Activity Assay

    fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt
    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using <t>4MUSia.</t> Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Fluorogenic Sialidase Substrate 2 4 Methylumbelliferyl α D N Acetylneuraminic Acid Sodium Salt, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt/product/Gold Biotechnology Inc
    Average 91 stars, based on 1 article reviews
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    fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt - by Bioz Stars, 2024-05
    91/100 stars

    Images

    1) Product Images from "Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis * "

    Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M111.278135

    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Figure Legend Snippet: Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

    Techniques Used: Activity Assay, Staining, Concentration Assay

    BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.
    Figure Legend Snippet: BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

    Techniques Used: Incubation, MANN-WHITNEY, Activity Assay

    fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt  (Gold Biotechnology Inc)


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    Structured Review

    Gold Biotechnology Inc fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt
    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using <t>4MUSia.</t> Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Fluorogenic Sialidase Substrate 2 4 Methylumbelliferyl α D N Acetylneuraminic Acid Sodium Salt, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt/product/Gold Biotechnology Inc
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt - by Bioz Stars, 2024-05
    91/100 stars

    Images

    1) Product Images from "Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis * "

    Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M111.278135

    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Figure Legend Snippet: Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

    Techniques Used: Activity Assay, Staining, Concentration Assay

    BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.
    Figure Legend Snippet: BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

    Techniques Used: Incubation, MANN-WHITNEY, Activity Assay

    synthetic fluorogenic substrate fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt  (Gold Biotechnology Inc)


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    Structured Review

    Gold Biotechnology Inc synthetic fluorogenic substrate fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt
    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using <t>4MUSia.</t> Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Synthetic Fluorogenic Substrate Fluorogenic Sialidase Substrate 2 4 Methylumbelliferyl α D N Acetylneuraminic Acid Sodium Salt, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/synthetic fluorogenic substrate fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt/product/Gold Biotechnology Inc
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    synthetic fluorogenic substrate fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt - by Bioz Stars, 2024-05
    91/100 stars

    Images

    1) Product Images from "Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis * "

    Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M111.278135

    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Figure Legend Snippet: Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

    Techniques Used: Activity Assay, Staining, Concentration Assay

    BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.
    Figure Legend Snippet: BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

    Techniques Used: Incubation, MANN-WHITNEY, Activity Assay

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    Gold Biotechnology Inc 2 4 methylumbelliferyl n acetylneuraminic acid
    Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, <t>4-MU-Neu5Ac</t> assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).
    2 4 Methylumbelliferyl N Acetylneuraminic Acid, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Gold Biotechnology Inc synthetic fluorogenic substrate fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt
    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using <t>4MUSia.</t> Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Synthetic Fluorogenic Substrate Fluorogenic Sialidase Substrate 2 4 Methylumbelliferyl α D N Acetylneuraminic Acid Sodium Salt, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Gold Biotechnology Inc fluorogenic sialidase substrate 2 4 methylumbelliferyl α d n acetylneuraminic acid sodium salt
    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using <t>4MUSia.</t> Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.
    Fluorogenic Sialidase Substrate 2 4 Methylumbelliferyl α D N Acetylneuraminic Acid Sodium Salt, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, 4-MU-Neu5Ac assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).

    Journal: The Journal of Biological Chemistry

    Article Title: Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis

    doi: 10.1074/jbc.RA118.006221

    Figure Lengend Snippet: Sialidase activity and domain structure of G. vaginalis NanH1, NanH2, and NanH3. A, 4-MU-Neu5Ac assay of whole E. coli cultures expressing recombinant JCP8151B NanH1, NanH2, NanH3, or empty vector control. B, predicted domain structure of JCP8151B NanH1, NanH2, and NanH3. Putative catalytic residues are indicated above each protein. ConA, concanavalin A. C, JCP8151B NanH2 sialidase structural model showing conserved active-site residues, produced with Swissmodel and Deepview Swiss PDB viewer based on the sialidase crystal structure from M. viridifaciens (PDB code 1WCQ) (45).

    Article Snippet: 20 μl of each sample was mixed with 100 μl of 100 m m sodium acetate buffer (pH 5.5) containing 300 μ m 2-(4-methylumbelliferyl)- N -acetylneuraminic acid (4-MU-Neu5Ac, Gold Bio) in a black polypropylene assay plate (Eppendorf).

    Techniques: Activity Assay, Expressing, Recombinant, Plasmid Preparation, Produced

    NanH2 and NanH3 cleave 3′- and 6′-sialyllactose. A and B, preparations of NanH2 (A) or NanH3 (B) were mixed with 20 μm 3′-sialyllactose (3′ SL) or 6′-sialyllactose (6′ SL) and incubated at 37 °C for 3 h. At each time point, aliquots of the reaction mixtures were removed and analyzed by DMB-HPLC for free Neu5Ac.

    Journal: The Journal of Biological Chemistry

    Article Title: Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis

    doi: 10.1074/jbc.RA118.006221

    Figure Lengend Snippet: NanH2 and NanH3 cleave 3′- and 6′-sialyllactose. A and B, preparations of NanH2 (A) or NanH3 (B) were mixed with 20 μm 3′-sialyllactose (3′ SL) or 6′-sialyllactose (6′ SL) and incubated at 37 °C for 3 h. At each time point, aliquots of the reaction mixtures were removed and analyzed by DMB-HPLC for free Neu5Ac.

    Article Snippet: 20 μl of each sample was mixed with 100 μl of 100 m m sodium acetate buffer (pH 5.5) containing 300 μ m 2-(4-methylumbelliferyl)- N -acetylneuraminic acid (4-MU-Neu5Ac, Gold Bio) in a black polypropylene assay plate (Eppendorf).

    Techniques: Incubation

    NanH2 and NanH3 act on N-linked and O-linked sialoglycan substrates relevant to the host mucosa. A–D, sialoglycans included SIgA from human colostrum (A), BSM (B and C), and GBS whole cells (D). Preparations of NanH2 or NanH3 were mixed with each substrate and incubated at 37 °C for 4 h. AUS was used as a positive control. At each time point, aliquots of the reaction mixtures were removed and analyzed for Neu5Ac or N-glycolylneuraminic acid (Neu5Gc) by DMB-HPLC.

    Journal: The Journal of Biological Chemistry

    Article Title: Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis

    doi: 10.1074/jbc.RA118.006221

    Figure Lengend Snippet: NanH2 and NanH3 act on N-linked and O-linked sialoglycan substrates relevant to the host mucosa. A–D, sialoglycans included SIgA from human colostrum (A), BSM (B and C), and GBS whole cells (D). Preparations of NanH2 or NanH3 were mixed with each substrate and incubated at 37 °C for 4 h. AUS was used as a positive control. At each time point, aliquots of the reaction mixtures were removed and analyzed for Neu5Ac or N-glycolylneuraminic acid (Neu5Gc) by DMB-HPLC.

    Article Snippet: 20 μl of each sample was mixed with 100 μl of 100 m m sodium acetate buffer (pH 5.5) containing 300 μ m 2-(4-methylumbelliferyl)- N -acetylneuraminic acid (4-MU-Neu5Ac, Gold Bio) in a black polypropylene assay plate (Eppendorf).

    Techniques: Incubation, Positive Control

    Sialidase activity of isolated recombinant NanH proteins. A, 4-MU-Neu5Ac assay on JCP8151B NanH1 isolated from E. coli lysates. B, normalization of recombinant NanH1, NanH2, and NanH3 by SDS-PAGE and Coomassie staining. MW, molecular weight. C, end point assay showing release of sialic acids from 4-MU-Neu5Ac, BSM, colostrum SIgA, and sialyllactose in the presence of NanH1, NanH2, or NanH3. Samples were incubated at 37 °C for 2 h, and free sialic acids were measured by DMB-HPLC.

    Journal: The Journal of Biological Chemistry

    Article Title: Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis

    doi: 10.1074/jbc.RA118.006221

    Figure Lengend Snippet: Sialidase activity of isolated recombinant NanH proteins. A, 4-MU-Neu5Ac assay on JCP8151B NanH1 isolated from E. coli lysates. B, normalization of recombinant NanH1, NanH2, and NanH3 by SDS-PAGE and Coomassie staining. MW, molecular weight. C, end point assay showing release of sialic acids from 4-MU-Neu5Ac, BSM, colostrum SIgA, and sialyllactose in the presence of NanH1, NanH2, or NanH3. Samples were incubated at 37 °C for 2 h, and free sialic acids were measured by DMB-HPLC.

    Article Snippet: 20 μl of each sample was mixed with 100 μl of 100 m m sodium acetate buffer (pH 5.5) containing 300 μ m 2-(4-methylumbelliferyl)- N -acetylneuraminic acid (4-MU-Neu5Ac, Gold Bio) in a black polypropylene assay plate (Eppendorf).

    Techniques: Activity Assay, Isolation, Recombinant, SDS Page, Staining, Molecular Weight, End Point Assay, Incubation

    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

    Journal: The Journal of Biological Chemistry

    Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis

    doi: 10.1074/jbc.M111.278135

    Figure Lengend Snippet: Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

    Article Snippet: Kinetic Analysis of Sialidase Activity Using Synthetic Fluorogenic Substrate Fluorogenic sialidase substrate 2–4-methylumbelliferyl-α- d - N -acetylneuraminic acid sodium salt (4MUSia) from Gold BioTechnology was dissolved at 10 m m in water, aliquotted, and frozen at −80 °C.

    Techniques: Activity Assay, Staining, Concentration Assay

    BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

    Journal: The Journal of Biological Chemistry

    Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis

    doi: 10.1074/jbc.M111.278135

    Figure Lengend Snippet: BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

    Article Snippet: Kinetic Analysis of Sialidase Activity Using Synthetic Fluorogenic Substrate Fluorogenic sialidase substrate 2–4-methylumbelliferyl-α- d - N -acetylneuraminic acid sodium salt (4MUSia) from Gold BioTechnology was dissolved at 10 m m in water, aliquotted, and frozen at −80 °C.

    Techniques: Incubation, MANN-WHITNEY, Activity Assay

    Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

    Journal: The Journal of Biological Chemistry

    Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis *

    doi: 10.1074/jbc.M111.278135

    Figure Lengend Snippet: Sialidase enzyme activity reflects microbiological status. BV status was assessed by Nugent scoring of Gram-stained vaginal smears (scores shown in parentheses). A, kinetics of sialidase activity was measured in vaginal swab elutions using 4MUSia. Briefly, sialidase activity was measured by combining one volume of BV sample with two volumes of substrate at 300 μm to give a final concentration of 200 μm in 100 mm sodium acetate buffer, pH 5.5. Representative data are shown. B, rates of 4MUSia hydrolysis are elevated in BV, whereas normal controls were sialidase negative. ***, p < 0.0001.

    Article Snippet: Fluorogenic sialidase substrate 2–4-methylumbelliferyl-α- d - N -acetylneuraminic acid sodium salt (4MUSia) from Gold BioTechnology was dissolved at 10 m m in water, aliquotted, and frozen at −80 °C.

    Techniques: Activity Assay, Staining, Concentration Assay

    BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

    Journal: The Journal of Biological Chemistry

    Article Title: Hydrolysis of Secreted Sialoglycoprotein Immunoglobulin A (IgA) in ex Vivo and Biochemical Models of Bacterial Vaginosis *

    doi: 10.1074/jbc.M111.278135

    Figure Lengend Snippet: BV sialidases act on sialic acids presented in multiple contexts relevant to the reproductive mucosa. BV specimens containing high levels of sialidase were incubated alongside matched controls (n = 14 each) with macromolecules bearing terminal sialic acids in different contexts. Released sialic acid was quantified by derivatization and HPLC as described in “Experimental Procedures” to assess the ability of BV sialidases to cleave different types of sialic acid-containing substrates. All of the data were normalized to total sialic acid (Neu5Ac) released by digestion with A. ureafaciens sialidase, shown in separate experiments to result in complete release as compared with acid hydrolysis. All of the substrates tested, including 2,3-linked sialic acids from the group B Streptococcus (GBS) capsule and primarily O-linked sialo-glycans from bovine submaxillary mucin (BSM), were desialylated to near completion by BV samples, whereas control specimens had little evidence of sialic acid hydrolysis. The Mann-Whitney U test was used to examine statistical significance (p < 0.0001 for all substrates; inset). The levels of sialidase activity (4MUSia) indicated for each sample are initial rates normalized relative to the sample with highest activity level.

    Article Snippet: Fluorogenic sialidase substrate 2–4-methylumbelliferyl-α- d - N -acetylneuraminic acid sodium salt (4MUSia) from Gold BioTechnology was dissolved at 10 m m in water, aliquotted, and frozen at −80 °C.

    Techniques: Incubation, MANN-WHITNEY, Activity Assay