07298
FabRICATOR®
for cleaving 2 mg IgG, 2000 U/vial
Synonym(s):
IdeS from Streptococcus pyogenes
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About This Item
UNSPSC Code:
12352204
EC Number:
3.4.22
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
Storage Class
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
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
Sialylation-independent mechanism involved in the amelioration of murine immune thrombocytopenia using intravenous gammaglobulin.
Leontyev, D., et al.
Transfusion, doi: 10-doi: 10 (2012)
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.
M Lišková et al.
Analytical and bioanalytical chemistry, 400(2), 369-379 (2011-02-08)
A number of biologically important molecules, such as DNA, proteins, and antibodies, are routinely conjugated with fluorescent tags for high-sensitivity analyses. Here, the application of quantum dots in the place of bright and size-tunable luminophores is studied. Several selected bioconjugation
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