推荐产品
表单
powder
比活
2000 U/vial
储存温度
−20°C
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单位定义
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.
分析说明
SDS gel electrophoresis ≥ 95 % purity
法律信息
FabRICATOR is a registered trademark of Genovis AB
应用
产品编号
说明
价格
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
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
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
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
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
Chromatograms
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