E2039
Chondroitinase AC from Flavobacterium heparinum
recombinant, expressed in E. coli, ≥200 units/mg protein, For Chondroitin Sulfate Analysis
Synonym(s):
Chondroitin AC lyase
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
recombinant
expressed in E. coli
Quality Level
conjugate
(Glucosaminoglycan)
Assay
≥90% (SDS-PAGE)
form
lyophilized solid
specific activity
≥200 units/mg protein
shipped in
dry ice
storage temp.
−20°C
Looking for similar products? Visit Product Comparison Guide
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.
Unit Definition
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).
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Storage Class Code
11 - Combustible Solids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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
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)
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
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
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service