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
存储类别
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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
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
Antonina Pechkovsky et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(19), E1724-E1733 (2013-04-25)
The adenovirus E4orf4 protein regulates the progression of viral infection, and when expressed alone in mammalian tissue culture cells it induces protein phosphatase 2A (PP2A)-B55- and Src-dependent cell death, which is more efficient in oncogene-transformed cells than in normal cells.
Ulrich von Pawel-Rammingen et al.
The EMBO journal, 21(7), 1607-1615 (2002-04-03)
Recent work from several laboratories has demonstrated that proteolytic mechanisms significantly contribute to the molecular interplay between Streptococcus pyogenes, an important human pathogen, and its host. Here we describe the identification, purification and characterization of a novel extracellular cysteine proteinase
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