Analytical Data
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基因名
gspB
- Application
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别名
gspB；Platelet binding Protein GspB
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种属
Human
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表达系统
E. coli
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标签
GST 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
Q939N5
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表达区间
233-617aa
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氨基酸序列
EASSQTGRRRTRRAVTESAPNVEYHDVKGDMIQSVTTSFDDTSRLLTWTINLTPRQVKSNLGALVSISGNQETRTVTINGKNAANGGVYNSGGAWNLYTGESVNNNVLRITTQVNDTGGEVKLGLRLVTSDKKITKTNLPLEFSQVAATTNGSWDKAGYNTTIVEKDTERPVVNVPSEITVYRGESFEYFATVTDNSNAFDLAKTVVRWLYNNQPGRGTEWLQYSVTQVGNQLKVRIFGNVPIDTTIGDYTRYVVATDAAGNVNATQTEMGNAAVDKTSVNGQFKLIIRFRIKTPENTVFVNNPNQLTEVEKNLVREAVKKSNPDLRAQDVLNSNYVTGITVSNNGTTTITYRDGRKDIIDGSKFIDTRAGSISKSQSTSNSISV
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分子量
68.5 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 the GspB protein, a surface adhesin found in Streptococcus gordonii, has garnered significant attention due to its role in bacterial pathogenesis and biofilm formation. GspB is a glycoprotein that binds to host tissues and contributes to the colonization of oral and gastrointestinal mucosa, making it crucial for the establishment of infections. Understanding GspB's structure and function could provide insights into the mechanisms of bacterial adherence and biofilm development, which are key factors in dental caries and other oral diseases. Moreover, GspB's potential as a vaccine target has spurred research into its immunogenic properties, as it could lead to novel prophylactic strategies against streptococcal infections. The recombinant expression of GspB allows for detailed analysis of its properties and interactions, paving the way for advanced therapeutic applications. This research not only enhances our understanding of microbial pathogenicity but also has implications for developing effective interventions to combat streptococcal-related diseases.
