Analytical Data
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Gene name
ideS
- Application
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Alternative Names
ideS；A-factor-processing enzyme
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
DSFSANQEIRYSEVTPYHVTSVWTKGVTPPAKFTQGEDVFHAPYVANQGWYDITKTFNGKDDLLCGAATAGNMLHWWFDQNKEKIEAYLKKHPDKQKIMFGDQELLDVRKVINTKGDQTNSELFNYFRDKAFPGLSARRIGVMPDLVLDMFINGYYLNVYKTQTTDVNRTYQEKDRRGGIFDAVFTRGDQSKLLTSRHDFKEKNLKEISDLIKKELTEGKALGLSHTYANVRINHVINLWGADFDSNGNLKAIYVTDSDSNASIGMKKYFVGVNSAGKVAISAKEIKEDNIGAQVLGLFTLSTGQDSWNQTN
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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, a gene encoding an immunoglobulin-degrading enzyme, has garnered significant attention due to its role in bacterial pathogenicity, particularly within Streptococcus pyogenes. This enzyme is known for its ability to cleave immunoglobulin G (IgG), thereby evading host immune responses and enhancing bacterial survival. Understanding ideS is critical for developing new therapeutic strategies against infections caused by S. pyogenes, which can lead to serious diseases, including rheumatic fever and necrotizing fasciitis. Research efforts have focused on characterizing the structure and function of ideS, as well as its enzymatic mechanisms, to explore potential inhibitors that could serve as novel antimicrobial agents. Given the increasing prevalence of antibiotic resistance, targeting virulence factors such as ideS represents a promising avenue for infection control. Additionally, recombinant forms of the ideS protein have been developed for use in various experimental settings, aiding in the elucidation of its biological functions and interactions with host immune components. This research not only aims to deepen our understanding of bacterial evasion strategies but also to pave the way for innovative therapeutic approaches that could improve disease outcomes and enhance public health initiatives.
