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Key Documents

E2039

Sigma-Aldrich

Chondroitinase AC from Flavobacterium heparinum

recombinant, expressed in E. coli, ≥200 units/mg protein, For Chondroitin Sulfate Analysis

Synonyme(s) :

Chondroitin AC lyase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in E. coli

Niveau de qualité

Conjugué

(Glucosaminoglycan)

Pureté

≥90% (SDS-PAGE)

Forme

lyophilized solid

Activité spécifique

≥200 units/mg protein

Conditions d'expédition

dry ice

Température de stockage

−20°C

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Application

Chondroitinase AC from Flavobacterium heparinum is an enzyme that cleaves sulfated and non-sulfated polysaccharide chains with (1-4) linkages between hexosamines and glucuronic acid residues, by an elimination mechanism. The resulting oligosaccharide products are mainly disaccharides with unsaturated uronic acids. Chondroitinase AC specifically degrades chondroitin sulfates A and C, but not chondroitin sulfate B (dermatan sulfate).
Chondroitinase AC has been applied to the analysis of chondroitin sulfate in commercial samples such as dietary supplements.
Highly purified to remove interferring β-glucuronidase and protease activities for use in the hydrolysis of chondroitin sulfate pror to HPLC analysis.

Définition de l'unité

1 unit is defined as the amount of enzyme that will liberate 1.0 μmole per minute of unsaturated disaccharides from chondroitin sulfate A at pH 6.7 at 37 °C as measured by the change in A232. The εμΜ for the reaction product Δ-Di-4S (chondroitin sulfates A and B) is 5.1 and 5.5 for Δ-Di-6S (chondroitin sulfate C).

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Determination of Chondroitin Sulfate Content in Raw Materials and Dietary Supplements by High-Performance Liquid Chromatography with Ultraviolet Detection After Enzymatic Hydrolysis: Single-Laboratory Validation
Ji, D., et al.
Journal - Association of Official Analytical Chemists, 90(3), 659-669 (2007)
E M Denholm et al.
European journal of pharmacology, 416(3), 213-221 (2001-04-06)
In the current study, two specific glycosaminoglycan lyases, chondroitinase AC and chondroitinase B, were utilized to examine the roles of chondroitin sulfates and dermatan sulfate in tumor metastasis and angiogenesis. Melanoma cells (SK-MEL) or endothelial cells were treated with either
Fernanda L Paganelli et al.
International journal of antimicrobial agents, 49(3), 355-363 (2017-02-12)
Enterococcus faecium is a multidrug-resistant (MDR) nosocomial pathogen causing significant morbidity in debilitated patients. New antimicrobials are needed to treat antibiotic-resistant E. faecium infections in hospitalised patients. E. faecium incorporates lipoteichoic acid (LTA) (1,3-polyglycerol-phosphate linked to glycolipid) in its cell
Studies on the enzyme chondroitinase: product structure and ion effects.
H I NAKADA et al.
Archives of biochemistry and biophysics, 94, 244-251 (1961-08-01)
K Pojasek et al.
Biochemical and biophysical research communications, 286(2), 343-351 (2001-08-14)
Glycosaminoglycans (GAGs) are a family of complex polysaccharides involved in a diversity of biological processes, ranging from cell signaling to blood coagulation. Chondroitin sulfate (CS) and dermatan sulfate (DS) comprise a biologically important subset of GAGs. Two of the important

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Uncover more about glycosaminoglycans and proteoglycans including the structure of glycosaminoglycans (GAGs), the different types of GAGs, and their functions.

Uncover more about glycosaminoglycans and proteoglycans including the structure of glycosaminoglycans (GAGs), the different types of GAGs, and their functions.

Uncover more about glycosaminoglycans and proteoglycans including the structure of glycosaminoglycans (GAGs), the different types of GAGs, and their functions.

Uncover more about glycosaminoglycans and proteoglycans including the structure of glycosaminoglycans (GAGs), the different types of GAGs, and their functions.

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