Millipore Sigma Vibrant Logo

362180 N-Glycosidase A, Almond

N-Glycosidase A, Almond MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Glycopeptidase A, PNGase A

View Products on Sigmaaldrich.com
362180
  
Retrieving price...
Price could not be retrieved
Minimum Quantity is a multiple of
Maximum Quantity is
Upon Order Completion More Information
You Saved ()
 
—
Request Pricing
—
Limited Availability Limited Availability
In Stock 
Discontinued
Limited Quantities Available
Availability to be confirmed
    Remaining : Will advise
      Remaining : Will advise
      Will advise
      Contact Customer Service
      Contact Customer Service

       

      Contact Customer Service

      Overview

      Replacement Information
      Description
      Overview

      This product has been discontinued.



      Native N-Glycosidase A from almonds. Cleaves N-glycan chains from glycopeptides, including those with α1,3-linked core fucose. This enzyme cleaves between GlcNAc and asparagine.
      Note: 1 mU = 1 milliunit.
      Catalogue Number362180
      Brand Family Calbiochem®
      SynonymsGlycopeptidase A, PNGase A
      References
      ReferencesMeans, R.E. and Desrosiers, R.C. 2000. J. Virol. 74, 11181.
      Fan, J.Q., and Lee, Y.C. 1997. J. Biol. Chem. 272, 27058.
      Altmann, F., et al. 1995. Glycoconj. J. 12, 84.
      Takahashi, N., and Nishibe, H. 1978. J. Biochem. 84, 1467.
      Product Information
      CAS number83534-39-8
      Unit of DefinitionOne unit is defined as the amount of enzyme that will catalyze the release of 1.0 µmol hybrid and high-mannose oligosaccharides from ovalbumin glycopeptide per min at 37°C, pH 5.0.
      EC number3.5.1.52
      FormLiquid
      FormulationIn 50 mM citrate/phosphate buffer, 50% glycerol, pH 5.0.
      Quality SegmentMQ100
      Applications
      Biological Information
      Specific Activity≥500 mU/mg protein
      Physicochemical Information
      Contaminantsα- and β-galactosidase, β-glucosidase: ≤0.1%; proteases: none detected
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Blue Ice Only
      Toxicity Standard Handling
      Storage -20°C
      Do not freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade ITEM Number
      Catalogue Number GTIN
      362180 0

      Documentation

      N-Glycosidase A, Almond SDS

      Title

      Safety Data Sheet (SDS) 

      N-Glycosidase A, Almond Certificates of Analysis

      TitleLot Number
      362180

      References

      Reference overview
      Means, R.E. and Desrosiers, R.C. 2000. J. Virol. 74, 11181.
      Fan, J.Q., and Lee, Y.C. 1997. J. Biol. Chem. 272, 27058.
      Altmann, F., et al. 1995. Glycoconj. J. 12, 84.
      Takahashi, N., and Nishibe, H. 1978. J. Biochem. 84, 1467.
      Data Sheet

      Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

      Revision13-September-2007 RFH
      SynonymsGlycopeptidase A, PNGase A
      DescriptionNative N-Glycosidase A from almonds. Cleaves N-glycan chains from glycopeptides, including those with α1,3-linked core fucose. This enzyme cleaves between GlcNAc and asparagine. Has an optimal pH of 4.0-6.0.
      FormLiquid
      FormulationIn 50 mM citrate/phosphate buffer, 50% glycerol, pH 5.0.
      Recommended reaction conditions
      Deglycosylation of Glycopeptides For assaying N-Glycosidase A Use 0.5 mU/ml N-Glycosidase A in 100 mM citrate / phosphate buffer, pH 5.0 with 0.1% BSA. Guideline used for unit definition: 10 µl of 100 µM ovalbumin glycopeptide was incubated with 10 µl 0.5 mU/ml N-Glycosidase A at 37°C for 60 min. Reaction products were quantified by absorption at 220 nm on reversed phase HPLC (5 µm ODS-Hypersil column) at 220 nm. For preparative digestion Incubate 0.2-0.5 mU N-Glycosidase A with 100 nmoles glycopeptide in 20-50 µl citrate/phosphate buffer without BSA for 24 hrs at 37°C. Deglycosylation of Glycoproteins Various reagents such as 0.75 M β-mercaptethanol, 2% Triton X-100, 2% Tween®-80 detergent may be required to denature substrates sufficiently for deglycosylation. Enzyme activity may be significantly increased by addition of Mg2+, Zn2+, Co3+, or Cu3+. A guideline is 4 µglycoprotein incubated with 1 mU N-Glycosidase A in 10 mM sodium acetate, 0.5 M NaSCN, 0.1 M β-mercaptoethanol, pH 5.1, for 24 h at 37°C. However the nature of the glycoprotein substrate will determine optimal conditions. References Taga, E.M. et al. 1984. Biochemistry 23, 815. Tarentino, A.L. and Plummer, T.H. 1982. J. Biol. Chem. 257, 10776. Takahashi, N. and Nishibe, H. 1981. Biochim. Biophys. Acta 657, 457
      CAS number83534-39-8
      EC number3.5.1.52
      Contaminantsα- and β-galactosidase, β-glucosidase: ≤0.1%; proteases: none detected
      Specific activity≥500 mU/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will catalyze the release of 1.0 µmol hybrid and high-mannose oligosaccharides from ovalbumin glycopeptide per min at 37°C, pH 5.0.
      Storage -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-20°C).
      Toxicity Standard Handling
      ReferencesMeans, R.E. and Desrosiers, R.C. 2000. J. Virol. 74, 11181.
      Fan, J.Q., and Lee, Y.C. 1997. J. Biol. Chem. 272, 27058.
      Altmann, F., et al. 1995. Glycoconj. J. 12, 84.
      Takahashi, N., and Nishibe, H. 1978. J. Biochem. 84, 1467.