跳转至内容
Merck
CN

07298

Sigma-Aldrich

FabRICATOR®

for cleaving 2 mg IgG, 2000 U/vial

别名:

IdeS from Streptococcus pyogenes

登录查看公司和协议定价

关于此项目

EC 号:
3.4.22
UNSPSC代码:
12352204
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助
技术服务
需要帮助?我们经验丰富的科学家团队随时乐意为您服务。
让我们为您提供帮助

表单

powder

比活

2000 U/vial

储存温度

−20°C

正在寻找类似产品? 访问 产品对比指南

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

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

没有发现合适的版本?

如果您需要特殊版本,可通过批号或批次号查找具体证书。

已有该产品?

在文件库中查找您最近购买产品的文档。

访问文档库

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

我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.

联系客户支持