07298
FabRICATOR®
for cleaving 2 mg IgG, 2000 U/vial
Synonym(s):
IdeS from Streptococcus pyogenes
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About This Item
Enzyme Commission number:
3.4.22
UNSPSC Code:
12352204
Recommended Products
form
powder
specific activity
2000 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
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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
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
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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