β-cellobiose

α-D-Cellobiose octaacetate, 98% (alpha-D-Cellobiose octaacetate, 98%) serves as a substrate for glycosidases and is also used in carbohydrate biology research.

4-Methylumbelliferyl-β-D-cellobiose heptaacetate is a reagent used in biochemical reactions.

Acetobromocellobiose is a biochemical reagent that can be used as a biomaterial for life science related research and as a sulfonylation reagent for organic synthesis and drug discovery.

β-Glucosidase, Clostridium thermocellum (EC 3.2.1.21), is a glucosidase enzyme that targets β1→4 glycosidic bonds connecting two glucose or glucose-substituted molecules, such as cellobiose. This exocellulase enzyme is specific to various β-D-glycoside substrates. It catalyzes the hydrolysis of terminal non-reducing β-D-glucoside residues, releasing glucose.

β-Glucosidase, Bacteroides fragilis (EC 3.2.1.21), is a glucosidase enzyme that targets the β1→4 glycosidic bonds between two glucose molecules or glucose-substituted molecules, such as cellobiose. It serves as an exocellulase and exhibits specificity for various β-D-glucoside substrates. β-Glucosidase catalyzes the hydrolysis of the non-reducing terminal residues of β-D-glucosides, releasing glucose.

β-Glucanase 1(thermostable) is a glucosidase located at the brush border of the small intestine, targeting β1→4 glycosidic bonds between glucose or glucose-substituted molecules (such as the disaccharide cellobiose). This enzyme is an exocellulase specific to various β-D-glycosidic substrates. It catalyzes the hydrolysis of non-reducing terminal residues of β-D-glucosides, releasing glucose.

β-Glucosidase, Rhizobium etli (EC 3.2.1.21), is a glucosidase enzyme that targets β1→4 glycosidic bonds connecting two glucose or glucose-substituted molecules (such as disaccharide cellobiose). As an exocellulase, β-Glucosidase exhibits specificity for various β-D-glycoside substrates, catalyzing the hydrolysis of terminal non-reducing β-D-glucoside residues to release glucose.

β-Glucosidase (thermostable) is a glucose-metabolizing enzyme found in the brush border of the small intestine, targeting the β1→4 glycosidic bonds joining two glucose or glucose-substituted molecules, such as in disaccharides like cellobiose. This enzyme functions as an exocellulase with specificity for various β-D-glycoside substrates. It facilitates the hydrolysis of terminal non-reducing residues in β-D-glucosides, resulting in the release of glucose.

p-Aminophenyl β-D-cellobioside is an effective affinity ligand for cellobiose-degrading enzymes.