E7642
Endoglycosidase H from Streptomyces plicatus
recombinant, expressed in E. coli, buffered aqueous solution
Synonym(s):
β-N-Acetylglucosaminidase H
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
recombinant
expressed in E. coli
form
buffered aqueous solution
mol wt
27 kDa
storage temp.
2-8°C
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Unit Definition
One unit will hydrolyze 1.0 μmole of dabsyl-Asn-(GlcNAc)2(Man)5 per min at pH 5.5 at 37 °C.
Physical form
Solution in 0.05 M sodium phosphate, pH 7, containing 25 mM EDTA and preservative
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Rhizomucor miehei aspartic proteinases having improved properties.
M K Harboe
Advances in experimental medicine and biology, 436, 293-296 (1998-04-30)
John E Schiel et al.
Journal of mass spectrometry : JMS, 46(7), 649-657 (2011-06-28)
The current project describes the chemoenzymatic modification of bovine ribonuclease B (RNase B) to contain a single glycosylation site with a known glycan. A reactive disaccharide oxazoline derivative was synthesized and stereospecifically added to deglycosylated RNase B through endo-β-N-acetylglucosaminidase M
Yoshinobu Kimura et al.
Bioscience, biotechnology, and biochemistry, 75(5), 1019-1021 (2011-05-21)
Endo-β-N-acetylglucosaminidase (ENGase) is involved in the production of high-mannose type free N-glycans during plant development and fruit maturation. In a previous study (K. Nakamura et al. Biosci. Biotechnol. Biochem., 73, 461-464 (2009)), we identified the tomato ENGase gene and found
Wei Zhang et al.
Talanta, 85(1), 499-505 (2011-06-08)
Endoglycosidase is a class of glycosidases that specifically cleaves the glycosidic bond between two proximal residues of GlcNAc in the pentasaccharide core of N-glycan, leaving the innermost GlcNAc still attached to its parent protein, which provides a different diagnostic maker
Helena Ryšlavá et al.
The FEBS journal, 278(14), 2469-2484 (2011-05-14)
Fungal β-N-acetylhexosaminidases are inducible extracellular enzymes with many biotechnological applications. The enzyme from Penicillium oxalicum has unique enzymatic properties despite its close evolutionary relationship with other fungal hexosaminidases. It has high GalNAcase activity, tolerates substrates with the modified N-acyl group
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