C8058
Chondroitinase B from Flavobacterium heparinum
lyophilized powder (with BSA as stabilizer)
Sinónimos:
Chondroitin sulfate B lyase
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Acerca de este artículo
Biological source:
bacterial (Flavobacterium heparinum)
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Permítanos ayudarlebiological source
bacterial (Flavobacterium heparinum)
conjugate
(Glucosaminoglycan)
form
lyophilized powder (with BSA as stabilizer)
shipped in
dry ice
storage temp.
−20°C
Quality Level
Categorías relacionadas
Application
Chondroitinase B from Flavobacterium heparinum has been used in a study to assess the structural characterization and antithrombin activity of dermatan sulfate. Chondroitinase B from Flavobacterium heparinum has also been used in a study to investigate the chondroitin lyase action pattern via liquid chromatography–mass spectrometry.
The enzyme from Sigma has been used for the analysis of the frequency of iduronic acid in dermatan sulfate dodecasaccharide. It has also been used to digest dermatan sufate (DS) in melanoma cells. This digestion resulted in decreased proliferation and invasiveness of tumor cells, thereby suggesting a role for DS in metastasis.
Biochem/physiol Actions
Chondroitinase B degrades only chondroitin sulphate B producing oligo- and tetra-saccharides, and an unsaturated 4-sulphated disaccharide. It has an optimum temperature of 20 °C and an optimum pH of 8.0. The enzyme activity is inhibited by 50% using 0.1 M NaCI. Co2+, Fe3+ and Ba2+ also inhibit its activity.
Other Notes
One unit will form 0.1 μmole of unsaturated uronic acid per hr at pH 7.5 at 25°C using chondroitin sulfate B as substrate.
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2
Clase de almacenamiento
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Yvette M Coulson-Thomas et al.
Journal of neuroscience methods, 171(1), 19-29 (2008-04-18)
Injury to the CNS of vertebrates leads to the formation of a glial scar and production of inhibitory molecules, including chondroitin sulphate proteoglycans. Various studies suggest that the sugar component of the proteoglycan is responsible for the inhibitory role of
Y M Michelacci et al.
The Biochemical journal, 151(1), 121-129 (1975-10-01)
A chondroitinase that degrades only chondroitin sulphate B was isolated from Flavobacterium heparinum, and separated from a constitutive chondroitinase AC also present in extracts of F. heparinum. The enzyme acts only on chondroitin sulphate B, producing oligo- and tetra-saccharides, plus
Zhenqing Zhang et al.
Analytical biochemistry, 385(1), 57-64 (2008-11-11)
Liquid chromatography-mass spectrometry was applied to determine the action pattern of different chondroitin lyases. Two commercial enzymes, chondroitinase ABC (Proteus vulgaris) and chondroitinase ACII (Arthrobacter aurescens), having action patterns previously determined by viscosimetry and gel electrophoresis were first examined. Next
Gerdy B ten Dam et al.
The American journal of pathology, 171(4), 1324-1333 (2007-08-25)
Chondroitin sulfate (CS) is abundantly present in the tumor stroma, and tumor-specific CS modifications might be potential targets to influence tumor development. We applied the phage display technology to select antibodies that identify these tumor-specific CS modifications. Antibody GD3G7 was
Kristen R Taylor et al.
The Journal of biological chemistry, 280(7), 5300-5306 (2004-11-26)
Glycosaminoglycans have been implicated in the binding and activation of a variety of growth factors, cytokines, and chemokines. In this way, glycosaminoglycans are thought to participate in events such as development and wound repair. In particular, heparin and heparan sulfate
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QC Methods
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