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362180 N-Glycosidase A, Almond

362180
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
362180-5MIU Plastic ampoule 5 miu
Description
OverviewNative 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, 7558-79-4, 77-92-9, 56-81-5
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 LevelMQ100
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

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, 7558-79-4, 77-92-9, 56-81-5
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.