77661
FabRICATOR®
for cleaving 5 mg IgG, 5000 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
recombinant
expressed in E. coli
form
powder
specific activity
5000 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
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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
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
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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