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Merck
CN

07298

Sigma-Aldrich

FabRICATOR®

for cleaving 2 mg IgG, 2000 U/vial

别名:

IdeS from Streptococcus pyogenes

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关于此项目

EC 号:
3.4.22
UNSPSC代码:
12352204
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表单

powder

比活

2000 U/vial

储存温度

−20°C

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分析说明

SDS gel electrophoresis ≥ 95 % purity

其他说明

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.

法律信息

FabRICATOR is a registered trademark of Genovis AB

储存分类代码

13 - Non Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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
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
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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