Analytical Data
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基因名
ideS
- Application
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别名
ideS；A-factor-processing enzyme
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
F8V4V0
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表达区间
30-341aa
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氨基酸序列
DSFSANQEIRYSEVTPYHVTSVWTKGVTPPAKFTQGEDVFHAPYVANQGWYDITKTFNGKDDLLCGAATAGNMLHWWFDQNKEKIEAYLKKHPDKQKIMFGDQELLDVRKVINTKGDQTNSELFNYFRDKAFPGLSARRIGVMPDLVLDMFINGYYLNVYKTQTTDVNRTYQEKDRRGGIFDAVFTRGDQSKLLTSRHDFKEKNLKEISDLIKKELTEGKALGLSHTYANVRINHVINLWGADFDSNGNLKAIYVTDSDSNASIGMKKYFVGVNSAGKVAISAKEIKEDNIGAQVLGLFTLSTGQDSWNQTN
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分子量
36.9 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
