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
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Protein Description
The study of ideS recombination proteins has gained notable attention in the field of microbiology and immunology due to their critical role in bacterial pathogenesis, particularly in Streptococcus pyogenes. IdeS, an immunoglobulin G (IgG)-specific protease, is responsible for cleaving the Fc region of IgG antibodies, thereby evading the host immune response. This enzymatic activity not only facilitates bacterial survival and colonization but also impacts the outcome of infections and the efficacy of vaccine responses. Research into ideS has revealed its potential as a therapeutic target, as inhibiting its function could enhance host immunity against infections. Furthermore, understanding the molecular mechanisms of ideS expression and function can shed light on broader bacterial strategies for immune evasion. As scientists explore the structure-function relationship of ideS and investigate its interactions with host immune components, the findings could contribute to the development of novel antimicrobial strategies and improve our comprehension of host-pathogen dynamics. In summary, the ideS recombination protein serves as a key player in bacterial resistance mechanisms, highlighting its significance in infectious disease research and potential clinical applications.
