from Arthrobacter ureafaciens
For further processing only.
Neuraminidase (exo-α-Sialidase) material number and pack size: Material Number Pack Size 10269620103 custom fill
Neuraminidase removes terminal sialic acid residues from glycoproteins.
Solution in 10 mM sodium phosphate, 0.1% Micr-O-Protect (w/v), 0.25 mg/mL bovine serum albumin, pH 7.
Benefits of using in vitro glycoengeneeering to modify glycosylation of therapeutic proteins:
- Time- and cost-saving generation of glycan variants to develop improved drugs
- Optimized glycosylation without compromising other CQAs or product yield
- Improved lot-to-lot consistency to reduce risk of product quality variation and resulting delays
- Generation of glycoprofiles which may not otherwise be generated
- Streamlined analytics in comparability studies
- Neuraminidase can be used to hydrolyze terminal neuraminic acid residues from glycoproteins, such as monoclonal antibodies (MAB).
Cleaves terminal sialic-acid residues that are α2,3-, α2,6-, or α2,8-linked to Gal, GlcNAc, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids, or glycoproteins. Relative rate of cleavage is α2,6 >α2,3 >α2,8, determined on bonds in tri- and tetrasaccharides.
Appearance: clear, colorless solution
Composition: Na-phosphate 10 mmol/L; RPLA1 0.25 mg/mL; Micro-O-protect 01.% (w/v); pH approx. 7.0
pH value: 6.5-7.5
Activity (25°C; with AcNeu-lactose): ≥ 10 U/mL
Activity (37°C; with AcNeu-lactose): ≥ 16.7 U/mL
Protein (Bradford): 0.20 - 0.30 mg/mL
Contaminants expressed as percentage of neuraminidase activity:oteases (casein-resorufin) dA/17 h: ≤ 0.025
Stability at +2 to +8°C within specification range for 18 months
78:The sale of the Product does not exhaust or grant any rights in third party patents including patents of companies of the F. Hoffmann - La Roche AG group of companies, in particular, for the use of modified antibodies obtained by using the product.