36111
IgGZERO™
for cleaving 1 mg IgG, 1000 U/vial
Synonym(s):
EndoS from Streptococcus pyogenes
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About This Item
Recommended Products
form
powder
specific activity
1000 U/vial
storage temp.
−20°C
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Unit Definition
One unit is defined as the amount of enzyme required to remove 95% of 1 ug of human IgG Fc glycans in 30 minutes at 37°C, pH 7.2 as monitored by SDS-PAGE.
Analysis Note
SDS gel electrophoresis ≥ 95 % purity
Legal Information
IgGZERO is a trademark of Genovis AB
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Maria Allhorn et al.
Annals of the New York Academy of Sciences, 1173, 664-669 (2009-09-18)
The enzyme EndoS from Streptococcus pyogenes is an immunomodulatory molecule hydrolyzing the conserved glycans in the effector part of immunoglobulin G (IgG). EndoS is remarkably specific for IgG, and hydrolysis has profound effects on IgG effector functions. EndoS pretreatment of
Andrew M Goetze et al.
Molecular immunology, 49(1-2), 338-352 (2011-09-29)
A new method for simultaneously screening allelic variants and certain Fc modifications on endogenous human IgG1 and IgG2 directly from blood samples is described. The IdeS endoproteinase was used to cleave IgG in serum to generate Fc, which, after denaturation
Andrew M Goetze et al.
Glycobiology, 22(2), 221-234 (2011-09-21)
Glycation of immunoglobulin G (IgG) can result from incubation with a reducing sugar in vitro or during circulation in vivo. Upon injection of a recombinantly produced human therapeutic IgG into humans, changes in the glycation levels could be observed as
Patrick R Romano et al.
Biochemical and biophysical research communications, 414(1), 84-89 (2011-09-29)
Changes in glycosylation have long been associated with disease. While there are many methods to detect changes in glycosylation, plant derived lectins are often used to determine changes on specific proteins or molecules of interest. One change in glycosylation that
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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