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Endoglycosidase H

ROCHE/ENDOH-RO - recombinant form of the gene from Streptomyces plicatus

Synonym: Endo-β-N-acetylglucosaminidase H; glycosidase

Product Type: Chemical

Catalog Number PKG Qty. Price Quantity
45-11088726001 200 µL
$0.00
1/EA
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45-11643053001 500 µL
$0.00
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assay ≥90% (SDS-PAGE)
biological source Streptomyces sp. (S. plicatus)
conjugate (N-linked)
form solution
manufacturer/tradename Roche
mol wt Mr 29 kDa
optimum pH 5-6
packaging pkg of 200 μL (11088726001 [1U])
  pkg of 500 μL (11643053001 [2.5 U])
Quality Level 100 
specific activity ~40 units/mg protein (at +37°C and pH 5.5 with dabsyl-Asn(GlcNAc)2(Man)5 as the substrate)
storage temp. 2-8°C
Application: Use Endoglycosidase H for the deglycosylation of glycoproteins. Endo H has been used for the analysis of glycosylation of ATP-binding cassette proteins.
General description: Endo-β-N-acetylglucosaminidase H
Endoglycosidase H hydrolyzes N-linked oligosaccarides of glycopeptides/proteins. It cleaves only high mannose structures.
Other Notes: For life science research only. Not for use in diagnostic procedures.
Physical form: Solution in 50 mM sodium phosphate, 25 mM EDTA, 0.1% Micr-O-protect; (w/v), pH 7
Quality: Absence of contaminants: α- and β-glucosidase, β-galactosidase, α-mannosidase, β-N-acetyl-hexosaminidase, α-L-fucosidase, and proteases are not detectable.
Specificity: Active on N-linked oligosaccharides of glycopeptides/proteins.
Cleaves only high-mannose structures (n = 2 - 150, x = [Man]1-2, y = H), and hybrid structures (n = 2, x and/or y = AcNeu-Gal-GlcNAc).
Unit Definition: One unit enzyme activity hydrolyzes 1 μmol dabsyl-Asn(GlcNAc)2(Man)5 or 0.2 μmol dansyl-Asn (GlcNAc)2(Man)5 in one minute at 37 °C and pH 5.5.

Note: 5 U, using the dabsyl substrate, corresponds to 1 U using the dansyl substrate.
Purity ≥90% (SDS-PAGE)
activity specific activity: ~40 units/mg protein (at +37°C and pH 5.5 with dabsyl-Asn(GlcNAc)2(Man)5 as the substrate)
Storage Temp. 2-8°C
Enzyme Commission (EC) Number 3.2.1.96   ( BRENDA  | IUBMB  )
UNSPSC 12352200

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