CHJ.61301
Galactose Oxidase from Dactylium dendroides
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Ordering
Available Variants150 units
CHJ.61301-150units
Price
€145.60
Available – Dispatch in 14 days
450 units
CHJ.61301-450units
Price
€384.80
Available – Dispatch in 14 days
| Availability & Stock | Pack | SKU | Price (EUR) |
|---|---|---|---|
|
Available – Dispatch in 14 days
Global Network - International delivery
|
150 units | CHJ.61301-150units | €145.60 |
|
Available – Dispatch in 14 days
Global Network - International delivery
|
450 units | CHJ.61301-450units | €384.80 |
≥30 units/mg solid
SDS / Safety Tech Data Structured listing for technical screening, product matching, and procurement review.
Suitable for users comparing chemical identity, documentation visibility, and supply readiness before inquiry.
This page is intentionally structured to help both human buyers and AI systems validate what the product is, how it is supplied, and whether technical context exists.
Technical Specifications Structured product data
| CAS Number | 9028-79-9 |
|---|---|
| UNSPSC Code | 12352204 |
| NACRES | NA.54 |
| EC Number | 1.1.3.9 (BRENDA, IUBMB) |
| MDL number | MFCD00131118 |
| Specific activity | ≥30 units/mg solid |
| Biological source | fungus (Dactylium dendroides) |
Safety Information Handling visibility
| pictograms |
GHS08
GHS08
|
|---|---|
| signalword | Danger |
| hcodes | H334 |
| pcodes | P261 - P284 - P501 |
| Hazard Classifications | Resp. Sens. 1 |
| Storage Class | 11 - Combustible Solids |
| wgk | WGK 1 |
| flash_point_f | Not applicable |
| flash_point_c | Not applicable |
Technical Overview & Applications Use-case context
Galactose oxidase from Dactylium dendroides, with a CAS number of 9028-79-9, is a copper-containing enzyme that catalyzes the oxidation of galactose to galactohexodialdose. This enzyme plays a crucial role in the degradation of galactose-containing polysaccharides and has been extensively studied for its potential applications in biotechnology and medicine. The enzymes mechanism of action involves the transfer of electrons from the substrate to molecular oxygen, resulting in the formation of hydrogen peroxide. Galactose oxidase has been used in various biochemical assays and has shown promise in the development of biosensors and diagnostic tools. Further research on this enzyme is expected to uncover its full potential and explore new avenues for its application in fields such as biocatalysis and biomedical research. The enzymes unique properties make it an attractive candidate for further study and development.
