07298
FabRICATOR®
for cleaving 2 mg IgG, 2000 U/vial
Synonym(s):
IdeS from Streptococcus pyogenes
form
powder
specific activity
2000 U/vial
storage temp.
−20°C
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Analysis Note
SDS gel electrophoresis ≥ 95 % purity
Other Notes
One unit is defined as the amount of enzyme required to fragment 95% of 1 ug of human IgG in 30 minutes at 37°C, pH 6.6 as monitored by SDS-PAGE.
Legal Information
FabRICATOR is a registered trademark of Genovis AB
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Guillaume Chevreux et al.
Analytical biochemistry, 415(2), 212-214 (2011-05-21)
We describe a fast and informative method to investigate the posttranslational modifications of monoclonal antibodies (MAbs). The MAb is first digested by a specific enzyme that cleaves heavy chains under the hinge domain. After reduction of disulfide bridges, three polypeptide
Jennifer L Hess et al.
Journal of microbiological methods, 70(2), 284-291 (2007-06-05)
The immunoglobulin degrading enzyme of Streptococcus pyogenes, IdeS, is an unusual cysteine protease produced by group A streptococci for which the only known substrate is immunoglobulin G (IgG). To date, IdeS has not been found to cleave any of the
Motti Gerlic et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(19), 7808-7813 (2013-04-23)
Host innate immune responses to DNA viruses involve members of the nucleotide-binding domain, leucine-rich repeat and pyrin domain containing protein (NLRP) family, which form "inflammasomes" that activate caspase-1, resulting in proteolytic activation of cytokines interleukin (IL)-1β and IL-18. We hypothesized
Mary H Ryan et al.
Molecular immunology, 45(7), 1837-1846 (2007-12-26)
A comparative in vitro survey of physiologically relevant human and microbial proteinases defined a number of enzymes that induced specific hinge domain cleavage in human IgG1. Several of these proteinases have been associated with tumor growth, inflammation, and infection. A
Theo Rispens et al.
Journal of the American Chemical Society, 133(26), 10302-10311 (2011-06-02)
Immunoglobulin G (IgG) antibodies are symmetrical molecules that may be regarded as covalent dimers of 2 half-molecules, each consisting of a light chain and a heavy chain. Human IgG4 is an unusually dynamic antibody, with half-molecule exchange ("Fab-arm exchange") resulting
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