lectins  (Vector Laboratories)


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  • 93
    Name:
    N acetylgalactosamine
    Description:
    N acetygalactosamine sugar is provided for use as an inhibitor of lectin conjugate binding or for eluting glycoproteins or other glycoconjugates from columns of agarose lectins This sugar is supplied as a dry powder When reconstituted in 5 ml of water the resulting sugar solution is 100 mM
    Catalog Number:
    s-9001
    Price:
    None
    Category:
    Immunology or serology reagents or solutions or stains
    Size:
    5 ml
    Buy from Supplier


    Structured Review

    Vector Laboratories lectins
    N acetylgalactosamine
    N acetygalactosamine sugar is provided for use as an inhibitor of lectin conjugate binding or for eluting glycoproteins or other glycoconjugates from columns of agarose lectins This sugar is supplied as a dry powder When reconstituted in 5 ml of water the resulting sugar solution is 100 mM
    https://www.bioz.com/result/lectins/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    lectins - by Bioz Stars, 2021-03
    93/100 stars

    Images

    1) Product Images from "Infectious Pancreatic Necrosis Virus: Identification of a VP3-Containing Ribonucleoprotein Core Structure and Evidence for O-Linked Glycosylation of the Capsid Protein VP2"

    Article Title: Infectious Pancreatic Necrosis Virus: Identification of a VP3-Containing Ribonucleoprotein Core Structure and Evidence for O-Linked Glycosylation of the Capsid Protein VP2

    Journal: Journal of Virology

    doi:

    Detection of polypeptides and carbohydrates after alkaline β elimination. Lyophilized samples of IPNV, human Ad2, and transferrin (transf.) were incubated at 37°C for 20 h in 5 mM NaOH with 1 M NaBH 4 (+) or in PBS (−) as described in the text. Analysis by SDS–13% PAGE was followed by transblotting and detection with antiserum (αIPNV and αfiber are antibodies against the glycosylated 62-kDa fiber protein of Ad2) or with lectins (SBA and WGA). The amount of IPNV polypeptides applied to each lane was 0.37 μg, and those of the controls Ad2 and transf. were 3.3 and 0.5 μg, respectively.
    Figure Legend Snippet: Detection of polypeptides and carbohydrates after alkaline β elimination. Lyophilized samples of IPNV, human Ad2, and transferrin (transf.) were incubated at 37°C for 20 h in 5 mM NaOH with 1 M NaBH 4 (+) or in PBS (−) as described in the text. Analysis by SDS–13% PAGE was followed by transblotting and detection with antiserum (αIPNV and αfiber are antibodies against the glycosylated 62-kDa fiber protein of Ad2) or with lectins (SBA and WGA). The amount of IPNV polypeptides applied to each lane was 0.37 μg, and those of the controls Ad2 and transf. were 3.3 and 0.5 μg, respectively.

    Techniques Used: Incubation, Polyacrylamide Gel Electrophoresis, Whole Genome Amplification

    Effects of inhibitors of glycosylation. Virus-infected cells were treated with the following glycosylation inhibitors added at 1 h p.i.: 10-μg/ml tunicamycin (tun), 3 mM deoxymannojirimycin (dMM), and 4 mM N ) was applied, and three different lectins were selected for the detection of lectin-binding proteins (SBA, UEA, and ConA, recognizing GalNAc, fucose, and mannose, respectively). A polyclonal serum against IPNV was used for detection of viral proteins.
    Figure Legend Snippet: Effects of inhibitors of glycosylation. Virus-infected cells were treated with the following glycosylation inhibitors added at 1 h p.i.: 10-μg/ml tunicamycin (tun), 3 mM deoxymannojirimycin (dMM), and 4 mM N ) was applied, and three different lectins were selected for the detection of lectin-binding proteins (SBA, UEA, and ConA, recognizing GalNAc, fucose, and mannose, respectively). A polyclonal serum against IPNV was used for detection of viral proteins.

    Techniques Used: Infection, Binding Assay

    2) Product Images from "Infectious Pancreatic Necrosis Virus: Identification of a VP3-Containing Ribonucleoprotein Core Structure and Evidence for O-Linked Glycosylation of the Capsid Protein VP2"

    Article Title: Infectious Pancreatic Necrosis Virus: Identification of a VP3-Containing Ribonucleoprotein Core Structure and Evidence for O-Linked Glycosylation of the Capsid Protein VP2

    Journal: Journal of Virology

    doi:

    Detection of polypeptides and carbohydrates after alkaline β elimination. Lyophilized samples of IPNV, human Ad2, and transferrin (transf.) were incubated at 37°C for 20 h in 5 mM NaOH with 1 M NaBH 4 (+) or in PBS (−) as described in the text. Analysis by SDS–13% PAGE was followed by transblotting and detection with antiserum (αIPNV and αfiber are antibodies against the glycosylated 62-kDa fiber protein of Ad2) or with lectins (SBA and WGA). The amount of IPNV polypeptides applied to each lane was 0.37 μg, and those of the controls Ad2 and transf. were 3.3 and 0.5 μg, respectively.
    Figure Legend Snippet: Detection of polypeptides and carbohydrates after alkaline β elimination. Lyophilized samples of IPNV, human Ad2, and transferrin (transf.) were incubated at 37°C for 20 h in 5 mM NaOH with 1 M NaBH 4 (+) or in PBS (−) as described in the text. Analysis by SDS–13% PAGE was followed by transblotting and detection with antiserum (αIPNV and αfiber are antibodies against the glycosylated 62-kDa fiber protein of Ad2) or with lectins (SBA and WGA). The amount of IPNV polypeptides applied to each lane was 0.37 μg, and those of the controls Ad2 and transf. were 3.3 and 0.5 μg, respectively.

    Techniques Used: Incubation, Polyacrylamide Gel Electrophoresis, Whole Genome Amplification

    Effects of inhibitors of glycosylation. Virus-infected cells were treated with the following glycosylation inhibitors added at 1 h p.i.: 10-μg/ml tunicamycin (tun), 3 mM deoxymannojirimycin (dMM), and 4 mM N ) was applied, and three different lectins were selected for the detection of lectin-binding proteins (SBA, UEA, and ConA, recognizing GalNAc, fucose, and mannose, respectively). A polyclonal serum against IPNV was used for detection of viral proteins.
    Figure Legend Snippet: Effects of inhibitors of glycosylation. Virus-infected cells were treated with the following glycosylation inhibitors added at 1 h p.i.: 10-μg/ml tunicamycin (tun), 3 mM deoxymannojirimycin (dMM), and 4 mM N ) was applied, and three different lectins were selected for the detection of lectin-binding proteins (SBA, UEA, and ConA, recognizing GalNAc, fucose, and mannose, respectively). A polyclonal serum against IPNV was used for detection of viral proteins.

    Techniques Used: Infection, Binding Assay

    Related Articles

    Inhibition:

    Article Title: The Major Surface Glycoprotein of Pneumocystis murina Does Not Activate Dendritic Cells
    Article Snippet: Both MMR and DC-SIGN bound to P. murina Msg , although MMR binding was of borderline significance ( P = .053); binding of both was inhibited by mannan. .. In limited studies, other sugars, including, mannose, fucose, galactose, sialic acid, N-acetylglucosamine, and N-acetylgalactosamine, did not show consistent inhibition. .. Because the concanavalin A–purified P. murina Msg preparations may contain other Pneumocystis or host proteins, we repeated the binding experiments by using preparations of P. carinii Msg that were purified with a monoclonal antibody column.

    Binding Assay:

    Article Title: Infectious Pancreatic Necrosis Virus: Identification of a VP3-Containing Ribonucleoprotein Core Structure and Evidence for O-Linked Glycosylation of the Capsid Protein VP2
    Article Snippet: .. Although the binding capacity differed from lectin to lectin, it was clear that lectins preferentially recognizing N -acetylgalactosamine (GalNAc), e.g., Dolichos biflorus agglutinin, jacalin, peanut agglutinin, soybean agglutinin (SBA), and Vicia villosa agglutinin, bound significantly stronger than lectins with their highest specificity toward N -acetylglucosamine (GlcNAc), e.g., Bandeiraea simplicifolia lectin, Datura stramonium lectin, Lycopersicon esculentum lectin, Solanum tuberosum lectin, and wheat germ agglutinin (WGA) ( ; Vector Laboratories). ..

    Article Title: Characterization of Glycoconjugates of Extracellular Polymeric Substances in Tufa-Associated Biofilms by Using Fluorescence Lectin-Binding Analysis ▿Characterization of Glycoconjugates of Extracellular Polymeric Substances in Tufa-Associated Biofilms by Using Fluorescence Lectin-Binding Analysis ▿ †
    Article Snippet: In this method, the staining efficiency is much better than that of samples incubated in a petri dish. .. The carbohydrate binding specificities of selected lectins (AAL, HMA, LEA, LcH, PNA, and WGA; see Table 2) were evaluated by competitive-inhibition assays, using the carbohydrates galactose, N -acetylgalactosamine, N -acetylglucosamine, fucose, α-methyl mannoside, α-methyl glucoside, chitin hydrolysate, and N -acetyl neuraminic acid (Vector Laboratories, Burlingame, CA). .. The carbohydrates were incubated for 30 min prior to the staining procedure in the lectin staining solutions at concentrations recommended by the supplier (20 μg ml−1 ) in the dark at room temperature.

    Whole Genome Amplification:

    Article Title: Infectious Pancreatic Necrosis Virus: Identification of a VP3-Containing Ribonucleoprotein Core Structure and Evidence for O-Linked Glycosylation of the Capsid Protein VP2
    Article Snippet: .. Although the binding capacity differed from lectin to lectin, it was clear that lectins preferentially recognizing N -acetylgalactosamine (GalNAc), e.g., Dolichos biflorus agglutinin, jacalin, peanut agglutinin, soybean agglutinin (SBA), and Vicia villosa agglutinin, bound significantly stronger than lectins with their highest specificity toward N -acetylglucosamine (GlcNAc), e.g., Bandeiraea simplicifolia lectin, Datura stramonium lectin, Lycopersicon esculentum lectin, Solanum tuberosum lectin, and wheat germ agglutinin (WGA) ( ; Vector Laboratories). ..

    Article Title: Characterization of Glycoconjugates of Extracellular Polymeric Substances in Tufa-Associated Biofilms by Using Fluorescence Lectin-Binding Analysis ▿Characterization of Glycoconjugates of Extracellular Polymeric Substances in Tufa-Associated Biofilms by Using Fluorescence Lectin-Binding Analysis ▿ †
    Article Snippet: In this method, the staining efficiency is much better than that of samples incubated in a petri dish. .. The carbohydrate binding specificities of selected lectins (AAL, HMA, LEA, LcH, PNA, and WGA; see Table 2) were evaluated by competitive-inhibition assays, using the carbohydrates galactose, N -acetylgalactosamine, N -acetylglucosamine, fucose, α-methyl mannoside, α-methyl glucoside, chitin hydrolysate, and N -acetyl neuraminic acid (Vector Laboratories, Burlingame, CA). .. The carbohydrates were incubated for 30 min prior to the staining procedure in the lectin staining solutions at concentrations recommended by the supplier (20 μg ml−1 ) in the dark at room temperature.

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  • 93
    Vector Laboratories lectins
    Detection of polypeptides and carbohydrates after alkaline β elimination. Lyophilized samples of IPNV, human Ad2, and transferrin (transf.) were incubated at 37°C for 20 h in 5 mM NaOH with 1 M NaBH 4 (+) or in PBS (−) as described in the text. Analysis by SDS–13% PAGE was followed by transblotting and detection with antiserum (αIPNV and αfiber are antibodies against the glycosylated 62-kDa fiber protein of Ad2) or with <t>lectins</t> (SBA and WGA). The amount of IPNV polypeptides applied to each lane was 0.37 μg, and those of the controls Ad2 and transf. were 3.3 and 0.5 μg, respectively.
    Lectins, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lectins/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    lectins - by Bioz Stars, 2021-03
    93/100 stars
      Buy from Supplier

    Image Search Results


    Detection of polypeptides and carbohydrates after alkaline β elimination. Lyophilized samples of IPNV, human Ad2, and transferrin (transf.) were incubated at 37°C for 20 h in 5 mM NaOH with 1 M NaBH 4 (+) or in PBS (−) as described in the text. Analysis by SDS–13% PAGE was followed by transblotting and detection with antiserum (αIPNV and αfiber are antibodies against the glycosylated 62-kDa fiber protein of Ad2) or with lectins (SBA and WGA). The amount of IPNV polypeptides applied to each lane was 0.37 μg, and those of the controls Ad2 and transf. were 3.3 and 0.5 μg, respectively.

    Journal: Journal of Virology

    Article Title: Infectious Pancreatic Necrosis Virus: Identification of a VP3-Containing Ribonucleoprotein Core Structure and Evidence for O-Linked Glycosylation of the Capsid Protein VP2

    doi:

    Figure Lengend Snippet: Detection of polypeptides and carbohydrates after alkaline β elimination. Lyophilized samples of IPNV, human Ad2, and transferrin (transf.) were incubated at 37°C for 20 h in 5 mM NaOH with 1 M NaBH 4 (+) or in PBS (−) as described in the text. Analysis by SDS–13% PAGE was followed by transblotting and detection with antiserum (αIPNV and αfiber are antibodies against the glycosylated 62-kDa fiber protein of Ad2) or with lectins (SBA and WGA). The amount of IPNV polypeptides applied to each lane was 0.37 μg, and those of the controls Ad2 and transf. were 3.3 and 0.5 μg, respectively.

    Article Snippet: Although the binding capacity differed from lectin to lectin, it was clear that lectins preferentially recognizing N -acetylgalactosamine (GalNAc), e.g., Dolichos biflorus agglutinin, jacalin, peanut agglutinin, soybean agglutinin (SBA), and Vicia villosa agglutinin, bound significantly stronger than lectins with their highest specificity toward N -acetylglucosamine (GlcNAc), e.g., Bandeiraea simplicifolia lectin, Datura stramonium lectin, Lycopersicon esculentum lectin, Solanum tuberosum lectin, and wheat germ agglutinin (WGA) ( ; Vector Laboratories).

    Techniques: Incubation, Polyacrylamide Gel Electrophoresis, Whole Genome Amplification

    Effects of inhibitors of glycosylation. Virus-infected cells were treated with the following glycosylation inhibitors added at 1 h p.i.: 10-μg/ml tunicamycin (tun), 3 mM deoxymannojirimycin (dMM), and 4 mM N ) was applied, and three different lectins were selected for the detection of lectin-binding proteins (SBA, UEA, and ConA, recognizing GalNAc, fucose, and mannose, respectively). A polyclonal serum against IPNV was used for detection of viral proteins.

    Journal: Journal of Virology

    Article Title: Infectious Pancreatic Necrosis Virus: Identification of a VP3-Containing Ribonucleoprotein Core Structure and Evidence for O-Linked Glycosylation of the Capsid Protein VP2

    doi:

    Figure Lengend Snippet: Effects of inhibitors of glycosylation. Virus-infected cells were treated with the following glycosylation inhibitors added at 1 h p.i.: 10-μg/ml tunicamycin (tun), 3 mM deoxymannojirimycin (dMM), and 4 mM N ) was applied, and three different lectins were selected for the detection of lectin-binding proteins (SBA, UEA, and ConA, recognizing GalNAc, fucose, and mannose, respectively). A polyclonal serum against IPNV was used for detection of viral proteins.

    Article Snippet: Although the binding capacity differed from lectin to lectin, it was clear that lectins preferentially recognizing N -acetylgalactosamine (GalNAc), e.g., Dolichos biflorus agglutinin, jacalin, peanut agglutinin, soybean agglutinin (SBA), and Vicia villosa agglutinin, bound significantly stronger than lectins with their highest specificity toward N -acetylglucosamine (GlcNAc), e.g., Bandeiraea simplicifolia lectin, Datura stramonium lectin, Lycopersicon esculentum lectin, Solanum tuberosum lectin, and wheat germ agglutinin (WGA) ( ; Vector Laboratories).

    Techniques: Infection, Binding Assay