Recombinant F. meningosepticum Endo F1 Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 5220-GH
Key Product Details
- R&D Systems E. coli-derived Recombinant F. meningosepticum Endo F1 Protein (5220-GH)
- Quality control testing to verify active proteins with lot specific assays by in-house scientists
- All R&D Systems proteins are covered with a 100% guarantee
Product Specifications
Source
Arg31-Trp339, with an N-terminal Met and 6-His tag
Accession # P36911
Purity
Endotoxin Level
N-terminal Sequence Analysis
Predicted Molecular Mass
SDS-PAGE
Activity
The DC50 is < 5 ng. The DC50 is defined as the amount of enzyme required to remove 50% of glycan on 1 μg of RNase B in 30 minutes at
37 °C. . Use of Recombinant F. meningosepticum
Endo F1 in the delycoslyation of other substrates may require alternative conditions for optimal performance.
Formulation, Preparation and Storage
5220-GH
| Formulation | Supplied as a 0.2 μm filtered solution in Tris and NaCl. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: Endo-beta-N-acetylglucosaminidase F1/Endo F1
N-glycans are commonly found on various glycoproteins. While peptide N-glycosidase from Flavobacterium meningosepticum (PNGase F) is widely used to release virtually all types of N-glycans under denaturing conditions, Endo-beta -N-acetylglucosaminidases from the same bacterial species, including Endo F1, can be used under native conditions to specifically release particular types of N-glycans (1, 2). Because these glycosidases hydrolyze the chitobiose core ofN-glycans, the released glycan products will contain one GlcNAc residue at their reducing ends with the other GlcNAc residue remaining attached to an asparagine residue on the glycoprotein. Endo F1 specifically releases oligomannose and hybrid but not complex type N-glycans from glycoproteins (3, 4). This enzyme is also suitable to deglycosylate substrates under denaturing conditions and remains active on sulfated and core fucosylated N-glycans at reduced rates (4).
References
- Maley, F. et al. (1989) Anal. Biochem. 180:195.
- Tarentino, A.L. et al. (1985) Biochemistry. 24:4665.
- Tarentino, A.L. et al. (1992) J. Biol. Chem. 267:3868.
- Trimble, R.B. and Tarentino, A.L. (1991) J. Biol. Chem. 266:1646.
Alternate Names
UniProt
Additional Endo-beta-N-acetylglucosaminidase F1/Endo F1 Products
Product Documents for Recombinant F. meningosepticum Endo F1 Protein, CF
Product Specific Notices for Recombinant F. meningosepticum Endo F1 Protein, CF
For research use only