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G0535 Sigma

Glycopeptidase A from almonds

buffered aqueous glycerol solution, ≥0.05 unit/mL

Synonym: N-linked-glycopeptide-(N-acetyl-β-D-glucosaminyl)-L-asparagine amidohydrolase, N-Glycosidase A, PNGase A

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Description

Biochem/physiol Actions

Hydrolyzes an N4-(acetyl-β-D-glycosaminyl)asparagine in which the N-acetyl-D-glucosamine residue may be further glycosylated, yielding a (substituted) N-acetyl-β-D-glucoaminylamine and the peptide containing an aspartic residue.

Unit Definition

One unit will hydrolyze 1.0 μmole of ovalbumin glycopeptide per min at pH 5.0 at 37°C.

Physical form

Solution in 50% glycerol containing 50 mM citrate-phosphate buffer, pH 5.0, and BSA.

Application

Glycopeptidase A from almonds is used for deglycosylation. It catalyzes the removal of N-linked oligosaccharide chains and converts Asn residue to Asp.

General description

Glycopeptidase found in almonds can be divided into three groups- A, B and C. the optimum pH value and the isoelectric point of glycopeptidase A is 6.0 and 7.7 respectively. It has a preference for glycopeptides with long chains. It is also capable of hydrolyzing intact glycoproteins such as, desialyted human transferrin, ovalbumin etc. These proteins cleave glycoproteins with asialocarbohydrate moieties at their β-aspartyl-glucosylamine linkages.

Price and Availability


Amplified Detection

Biomedical Applications
Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
1

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles

Articles

N-Linked Glycan Strategies

Use of the endoglycosidic enzyme PNGase F (N-Glycosidase F) is the most effective method of removing virtually all N-linked oligosaccharides from glycoproteins. PNGase F cleaves all asparagine-linked...
Glycobiology Analysis Manual, 2nd Edition
Keywords: Applications, Detergents, Digestions, Mass spectrometry, Methods, Nucleic acid denaturation, Proteomics

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Peer-Reviewed Papers
15

References

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