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2-Chloro-4-nitrophenyl-β-(1,3:1,4)-glucotetraoside

2-Chloro-4-nitrophenyl-beta-1-3-1-4-glucotetraoside O-CNPBG4
Product code: O-CNPBG4
€265.00

20 mg

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Available for shipping

Content: 20 mg
Shipping Temperature: Ambient
Storage Temperature: Below -10oC
Physical Form: Powder
Stability: > 10 years under recommended storage conditions
CAS Number: Not Applicable
Synonyms: 2-Chloro-4-nitrophenyl β-D-glucopyranosyl-(1→4)-β-D-glucopyranosyl-(1→4)-β-D-glucopyranosyl-(1→3)-β-D-glucopyranoside
Molecular Formula: C30H44CINO23
Molecular Weight: 822.1
Purity: > 97%
Substrate For (Enzyme): β-Glucanase/Lichenase
Assay Format: Spectrophotometer, Microplate, Auto-analyser
Detection Method: Absorbance
Wavelength (nm): 400-420

High purity 2-Chloro-4-nitrophenyl-β-(1,3:1,4)-glucotetraoside for use in research, biochemical enzyme assays and in vitro diagnostic analysis. This is a colourimetric substrate for the measurement of lichenase or mixed linkage β-glucanase (endo-1,3:1,4-β-D-glucanase) activity. As this substrate can also be hydrolysed by exo-acting β-glucanase/β-glucosidase enzymes, it is recommended only for the assay of pure lichenase solutions. The data sheet for the analogous trisaccharide substrate, 2-Chloro-4-nitrophenyl-β-(1,3:1,4)-glucotrioside (cat. no. O-CNPBG3), describes suitable assay conditions.

Documents
Certificate of Analysis
Safety Data Sheet
Booklet
Publications
Megazyme publication
Novel approaches to the automated assay of β-glucanase and lichenase activity.

Mangan, D., Liadova, A., Ivory, R. & McCleary, B. V. (2016). Carbohydrate Research, 435, 162-172.

We report herein the development of a novel assay procedure for the measurement of β-glucanase and lichenase (EC 3.2.1.73) in crude enzyme extracts. Two assay formats based on a) a direct cleavage or b) an enzyme coupled substrate were initially investigated. The ‘direct cleavage’ substrate, namely 4,6-O-benzylidene-2-chloro-4-nitrophenyl-β-31-cellotriosyl-β-glucopyranoside (MBG4), was found to be the more generally applicable reagent. This substrate was fully characterised using a crude malt β-glucanase extract, a bacterial lichenase (Bacillus sp.) and a non-specific endo-1,3(4)-β-glucanase from Clostridium thermocellum (EC 3.2.1.6). Standard curves were derived that allow the assay absorbance response to be directly converted to β-glucanase/lichenase activity on barley β-glucan. The specificity of MBG4 was confirmed by analysing the action of competing glycosyl hydrolases that are typically found in malt on the substrate. Manual and automated assay formats were developed for the analysis of a) β-glucanase in malt flour and b) lichenase enzyme extracts and the repeatability of these assays was fully investigated.

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Safety Information
Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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