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Recombinant F. meningosepticum Endo F1 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 5220-GH

R&D Systems, part of Bio-Techne
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5220-GH-050

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

Source

E. coli

Accession #

Conjugate

Unconjugated

Applications

Enzyme Activity

Product Specifications

Source

E. coli-derived f. meningosepticum Endo-beta-N-acetylglucosaminidase F1/Endo F1 protein
Arg31-Trp339, with an N-terminal Met and 6-His tag
Accession # P36911

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met

Predicted Molecular Mass

35 kDa

SDS-PAGE

35 kDa, under reducing conditions

Activity

Measured by its ability to deglycosylate ribonuclease B under native conditions.
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.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

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

  1. Maley, F. et al. (1989) Anal. Biochem. 180:195.
  2. Tarentino, A.L. et al. (1985) Biochemistry. 24:4665.
  3. Tarentino, A.L. et al. (1992) J. Biol. Chem. 267:3868.
  4. Trimble, R.B. and Tarentino, A.L. (1991) J. Biol. Chem. 266:1646.

Alternate Names

CDC II-a, EndobetaNacetylglucosaminidase F1

UniProt

Additional Endo-beta-N-acetylglucosaminidase F1/Endo F1 Products

Product Documents for Recombinant F. meningosepticum Endo F1 Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant F. meningosepticum Endo F1 Protein, CF

For research use only

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