All Photos(3)
Synonym(s):
IdeS from Streptococcus pyogenes
Enzyme Commission number:
3.4.22
UNSPSC Code:
12352204
Recommended Products
recombinant
expressed in E. coli
form
powder
specific activity
5000 U/vial
storage temp.
−20°C
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Unit Definition
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.
Analysis Note
SDS gel electrophoresis ≥ 95 % purity
Legal Information
FabRICATOR is a registered trademark of Genovis AB
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Katja Wenig et al.
Proceedings of the National Academy of Sciences of the United States of America, 101(50), 17371-17376 (2004-12-03)
Pathogenic bacteria have developed complex and diverse virulence mechanisms that weaken or disable the host immune defense system. IdeS (IgG-degrading enzyme of Streptococcus pyogenes) is a secreted cysteine endopeptidase from the human pathogen S. pyogenes with an extraordinarily high degree
Bjarne Vincents et al.
Biochemistry, 43(49), 15540-15549 (2004-12-08)
Streptococcus pyogenes, an important pathogen in humans, secretes an IgG specific endopeptidase named IdeS. To elucidate the mechanism that is responsible for this specificity, we have here characterized the activity of IdeS in detail. Both gamma chains of human IgG
Sialylation-independent mechanism involved in the amelioration of murine immune thrombocytopenia using intravenous gammaglobulin.
Leontyev, D., et al.
Transfusion, doi: 10-doi: 10 (2012)
Johnson Agniswamy et al.
The Journal of biological chemistry, 279(50), 52789-52796 (2004-10-07)
Group A Streptococcus has evolved numerous mechanisms to evade the host immune system to survive, disseminate, and cause disease. Recently a secreted protein named Mac-1 was identified and shown to enhance survival of the pathogen. A new variant of Mac-1
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
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