recombinant
expressed in E. coli
form
buffered aqueous solution
mol wt
27 kDa
storage temp.
2-8°C
Physical form
Solution in 0.05 M sodium phosphate, pH 7, containing 25 mM EDTA and preservative
Other Notes
One unit will hydrolyze 1.0 μmole of dabsyl-Asn-(GlcNAc)2(Man)5 per min at pH 5.5 at 37 °C.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
Liv Anette Bøhle et al.
FEMS microbiology letters, 325(2), 123-129 (2011-11-19)
It has been demonstrated previously that Enterococcus faecalis produces secreted endoglycosidases that enable the bacteria to remove N-linked glycans from glycoproteins. One enzyme potentially responsible for this activity is EF0114, comprising a typical GH18 endoglycosidase domain and a GH20 domain.
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
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
Shu-Quan Fan et al.
The Journal of biological chemistry, 287(14), 11272-11281 (2012-02-10)
Endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae (Endo-D) is an endoglycosidase capable of hydrolyzing the Fc N-glycan of intact IgG antibodies after sequential removal of the sialic acid, galactose, and internal GlcNAc residues in the N-glycan. Endo-D also possesses transglycosylation activity with sugar
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