E. coli HTRA, Protease Do (aa 27 - 474) [His], recombinant protein from E. coli
Recombinant E. coli HTRA/Protease Do, His-tagged was expressed in E. coli. Ala27-Gln474, with a C-terminal 10 His tag and ERSIGS sequence (Accession # NP_414703)
> 90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
2-8°C short term, -20°C long term
in higher temperatures DegP (HtrA) will function as a protease by the directed degradation of proteins and in lower temperatures as a chaperone by assisting the non-covalent folding or unfolding and the assembly or disassembly of other macromolecular structures. Furthermore, moonlighting proteins may exhibit different behaviors not only as a result of its location within a cell, but also the type of cell that the protein is expressed in.
As a heat shock protein and a serine protease, HTRA (Protease Do or the DegP protease) is indispensable for bacterial survival at temperatures above 42 °C. It is a periplasmic protein with a signal peptide of 26 amino acid residues. The mature protein contains two 90 amino acid PDZ domains, which start at residue 280. The serine proteaseb activity is inhibited by diisopropyl fluorophosphate or dichloroisocoumarin. Four human proteins have been identified that are homologous to E. coli HTRA and believed to play a role in arthritis, cell growth, unfolded stress response, apoptosis, aging, and tumor progression.
HTRA; Protease Do; DegP protease; E. coli HTRA protein; Escherichia coli Protease Do protein; E. coli; Escherichia