FIMC E.Coli
Description
FIMC E.Coli Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (37-241 a.a.) and having a molecular mass of 25kDa. The FIMC is purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MGVALGATRV IYPAGQKQEQ LAVTNNDENS TYLIQSWVEN ADGVKDGRFI VTPPLFAMKG KKENTLRILD ATNNQLPQDR ESLFWMNVKA IPSMDKSKLT ENTLQLAIIS RIKLYYRPAK LALPPDQAAE KLRFRRSANS LTLINPTPYY LTVTELNAGT RVLENALVPP MGESTVKLPS DAGSNITYRT INDYGALTPK MTGVME.
Product Science Overview
Chaperone proteins play a crucial role in assisting the proper folding of newly synthesized proteins and preventing their aggregation. One such chaperone protein is FimC, found in Escherichia coli (E. coli). This protein is particularly significant in the assembly of type-1 pili, which are essential for the adhesion of pathogenic E. coli strains to host cell surfaces.
FimC is a 23 kDa two-domain periplasmic chaperone protein. It is required for the assembly of type-1 pili, which are filamentous, highly oligomeric protein complexes anchored to the outer bacterial membrane . These pili mediate the adhesion of pathogenic E. coli strains to host cell surfaces and help them persist in macrophages .
Recombinant FimC protein is often produced with a His-tag at the N-terminus to facilitate purification. The recombinant protein corresponds to the amino acids 37-241 of the native FimC protein . The production of recombinant proteins in host cells like E. coli often leads to challenges such as misfolding and aggregation. To address these issues, chaperone proteins like FimC are co-overproduced to enhance the solubility and proper folding of the target proteins .
The overproduction of recombinant proteins in E. coli can lead to their misfolding and aggregation due to limitations in the chaperone capacity of the host cells. To overcome this, a two-step procedure involving the co-overproduction of chaperone networks has been developed. This approach has shown a significant increase in the solubility of various recombinant proteins . Chaperone proteins like FimC are integral to this process, ensuring that the recombinant proteins achieve their native conformation and remain soluble.
Recombinant FimC protein is used in various research applications, including studies on protein folding, assembly of type-1 pili, and the development of strategies to enhance the solubility of recombinant proteins. The ability to produce soluble and functional recombinant proteins is crucial for biotechnological applications, including drug development and industrial enzyme production.
