Ordering
Available Variants50 units
CHJ.49701-50units
Price
€288.80
Available – Dispatch in 14 days
100 units
CHJ.49701-100units
Price
€494.40
Available – Dispatch in 14 days
| Availability & Stock | Pack | SKU | Price (EUR) |
|---|---|---|---|
|
Available – Dispatch in 14 days
Global Network - International delivery
|
50 units | CHJ.49701-50units | €288.80 |
|
Available – Dispatch in 14 days
Global Network - International delivery
|
100 units | CHJ.49701-100units | €494.40 |
Removes N-linked glycans, suitable for mass spectrometry, from Elizabethkingia miricola
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 | 83534-39-8 |
|---|---|
| UNSPSC Code | 12352204 |
| NACRES | NA.32 |
| EC Number | 3.5.1.52 (BRENDA, IUBMB) |
| MDL number | MFCD06656235 |
| Specific activity | ≥20000 units/mg protein |
| Biological source | bacterial (Elizabethkingia miricola) |
Safety Information Handling visibility
| pictograms |
GHS08
 GHS08
|
|---|---|
| signalword | Danger |
| hcodes | H334 |
| pcodes | P261 - P284 - P501 |
| Hazard Classifications | Resp. Sens. 1 |
| Storage Class | 12 - Non Combustible Liquids |
| wgk | WGK 2 |
| flash_point_f | Not applicable |
| flash_point_c | Not applicable |
| ppe | Eyeshields, Gloves, multi-purpose combination respirator cartridge (US) |
Technical Overview & Applications Use-case context
PNGase F Glycosidase, with a CAS number of 83534-39-8, is a recombinant enzyme derived from Flavobacterium meningosepticum. This enzyme is specifically designed to cleave N-glycosidic bonds between asparagine and carbohydrate moieties in glycoproteins, resulting in the removal of intact glycan structures. The reaction catalyzed by PNGase F is highly efficient and can be performed under a variety of conditions, making it a valuable tool in glycoprotein analysis and research. The enzyme is commonly used in applications such as glycan profiling, glycoprotein characterization, and the study of protein-glycan interactions. By removing N-linked glycans, PNGase F enables researchers to investigate the role of glycosylation in protein function, stability, and cellular recognition, providing valuable insights into the complex biology of glycoproteins. Its high specificity and efficiency make PNGase F a widely used enzyme in biochemical and biotechnological research.
