Analytical Data
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Gene name
IdeS
- Application
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Alternative Names
Immunoglubulin-degrading enzyme
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Species
Streptococcus pyogenes
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Source
E. coli
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Tag
C- 11xHis
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
F8V4V0
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Expression Region
30-341aa
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Molecular Weight
36.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
IdeS (immunoglobulin G-degrading enzyme of Streptococcus pyogenes) is a glycosylated protease with significant implications in the field of immunology and therapeutic development. Initially discovered as a virulence factor in Streptococcus pyogenes, IdeS has garnered attention for its unique ability to specifically cleave immunoglobulin G (IgG) at a distinct site, thereby abrogating its effector functions. This property of IdeS has been exploited to modulate immune responses, making it a potential tool for treating autoimmune diseases, transplant rejection, and other conditions characterized by inappropriate IgG activity. Research focusing on the recombinant production of IdeS has advanced our understanding of its structure-function relationship, enzymatic activity, and the role of its glycosylation in modulating substrate specificity. Furthermore, studies have investigated the therapeutic applications of IdeS by engineering variants with enhanced properties, such as improved stability and altered specificity, which could pave the way for novel immunotherapies. Through ongoing investigations, IdeS serves as a model system for exploring how bacterial proteins can be harnessed to regulate human immune responses, thereby providing a promising avenue for innovative treatments in the realm of immunology.
