Analytical Data
-
基因名
fimG
- Application
-
别名
fimG;Protein FimG
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P08190
-
表达区间
24-167aa
-
氨基酸序列
ADVTITVNGKVVAKPCTVSTTNATVDLGDLYSFSLMSAGAASAWHDVALELTNCPVGTSRVTASFSGAADSTGYYKNQGTAQNIQLELQDDSGNTLNTGATKTVQVDDSSQSAHFPLQVRALTVNGGATQGTIQAVISITYTYS
-
分子量
22.3 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Protein Description
The fimbrial protein fimG is a significant focus of research in microbiology, particularly concerning its role in the pathogenicity of uropathogenic Escherichia coli (UPEC), a leading cause of urinary tract infections (UTIs). Fimbriae, which are hair-like appendages on the bacterial surface, facilitate adhesion to the host's uroepithelial cells, promoting colonization and persistent infection. FimG plays a crucial role in the assembly and stability of these fimbrial structures, as it is involved in the regulation of fimbrial gene expression and the organization of the fimbrial fibers. Recent studies have utilized recombinant protein techniques to express and purify fimG, enabling detailed structural and functional analyses. Understanding the molecular mechanisms by which fimG contributes to UPEC virulence not only provides insights into bacterial pathogenesis but also presents potential avenues for developing novel therapeutic strategies. By targeting fimbrial adhesins, researchers aim to create more effective treatments for UTIs, reducing the reliance on antibiotics and addressing the growing problem of antibiotic resistance. The ongoing research into fimG and fimbrial interactions underscores the significance of this protein in the broader context of bacterial infection and host interaction, highlighting the need for innovative approaches to combat UPEC-related diseases.












