Recombinant Escherichia coli Periplasmic serine endoprotease DegP(degP)

N-terminal 6xHis-tagged

48.8 kDa

DegP acts as a chaperone at low tperatures but switches to a peptidase (heat shock protein) at higher tperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolytic activity is essential for the survival of cells at elevated tperatures. It can degrade IciA, ada, casein, globin and PapA. DegP shares specificity with DegQ. DegP is also involved in the biogenesis of partially folded outer-mbrane proteins (OMP).

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20C/-80C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures

degP

Escherichia coli (strain K12)