lectins (Vector Laboratories)


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

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
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:

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

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:

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

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 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 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, 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 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, |