Chondroitinase ABC II, CAS No.9024-13-9

CAS: 9024-13-9 Cat. No.: C766319 EC Number: 266-042-9,232-777-9 PubChem CID: 168009893

GRADE & PURITY Bioactive, Recombinant, ActiBioPure™, High Performance, EnzymoPure™, expressed in E.coli；≥1000 U/mg enzyme powder; ≥2000 U/mg protein

Accession #

C7S340

Expression system

E. coli

Bioactivity

≥1000 U/mg enzyme powder; ≥2000 U/mg protein

Overview

Microbial derived chondroitin sulfate (CS)/dermatan sulfate (DS) sugar chain degrading enzymes (CSases) belong to polysaccharide lyases, which break the β -1,4-glycosidic bond between N-acetylglucosamine (GalNAc) and hexuronic acid (GlcUA/IdoUA) through a b-elimination reaction. At the same time, unsaturated double bonds are formed between the C4 and C5 carbon atoms of the uronic acid, which have characteristic absorption at 232 nm and can be conveniently used for oligosaccharide product analysis and detection. Commercialized CSases include CSase ABC from Proteus vulgaris, which can simultaneously degrade CS, DS, and HA. In fact, CSase ABC is a mixture of two enzymes, with CSase ABCI being a CS/DS endonuclease and CSase ABCII being a non reducing end exonuclease of CS/DS; CSase ACI and B from Flavobacterium heparinum, where CSase ACI is a CS and HA specific endonuclease, while the latter is a DS specific endonuclease; The CSase ACII from Arthrobacter auricens is another CS and HA specific degrading enzyme, but it is an exonuclease that can effectively cleave the enzyme labeled with tetrasaccharides at the reducing end of CS oligosaccharides after being fluorescently labeled. Therefore, it is particularly useful in CS oligosaccharides enzymatic sequencing. CS/DS lyase is not only an important tool enzyme for studying the structure-activity relationship of CS/DS and preparing CS/DS oligosaccharides, but also has significant clinical application value in the treatment of central nervous system injuries. We can provide customers with various CSases with different substrate selectivity, substrate degradation modes, and specifications according to their needs, meeting various needs such as CS/DS structural and functional analysis, product quality testing, heparin/heparan sulfate production and purification, and large-scale enzymatic hydrolysis preparation of CS and DS functional oligosaccharides.

Specifications

Product Name

Chondroitinase ABC II, CAS No.9024-13-9

Synonyms

Chondroitin sulfate Lyase | chondroitin-sulfate-ABC exolyase | chondroitin ABC eliminase | chondroitin ABC lyase | chondroitinase | chondroitinase ABC | chondroitin sulfate ABC exoeliminase | chondroitin sulfate ABC exolyase | chondroitin sulfate ABC lyas

Grade

ActiBioPure™, Bioactive, High Performance, Recombinant, EnzymoPure™

Specifications & Purity

Bioactive, Recombinant, ActiBioPure™, High Performance, EnzymoPure™, expressed in E.coli；≥1000 U/mg enzyme powder; ≥2000 U/mg protein

Biochemical and Physiological Mechanisms

Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion, and preferentially degrades the tetra- and hexasaccharide derivatives of chondroitin sulfate and dermatan sulfate produced by the chondroitin sulfate ABC endolyase, to yield the

Bioactivity

≥1000 U/mg enzyme powder; ≥2000 U/mg protein

Accession #

C7S340

CAS

9024-13-9

Enzyme Commission Number

EC 4.2.2.21

Molecule Type

Enzyme

Storage and Shipping

Concentration

expressed in E.coli；≥1000 U/mg enzyme powder; ≥2000 U/mg protein

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

Stability And Storage

Store at -20℃ long term (12 months). Store at -80℃ long term (24 months).Upon reconstitution, it is recommended to aliquot. Avoid freeze/thaw cycle.

Unit definition

The amount of enzyme required to produce 0.1 μmol of unsaturated uronic acid per hour under the conditions of pH 8.0 and 37°C.

References

1. Xiaoduo Zhao, Lumin Yang, Licheng Zhang, Le Ji, Shuanhong Ma, Feng Zhou.  (2024)  Novel biomimetic macromolecules system for highly efficient lubrication, ROS scavenging and osteoarthritis treatment.  COLLOIDS AND SURFACES B-BIOINTERFACES,      [PMID:38733647] [10.1016/j.colsurfb.2024.113956]