Peptidyl-prolyl cis-trans isomerase A (ppiA), Escherichia coli O6:H1, recombinant

Organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). Source: E.coli. Expression Region: 25-190aa. Protein Length: Full Length of Mature Protein. Tag Info: N-terminal 10xHis-SUMO-tagged and C-terminal Myc-tagged. Target Protein Sequence: AKGDPHVLLT TSAGNIELEL DKQKAPVSVQ NFVDYVNSGF YNNTTFHRVI PGFMIQGGGF TEQMQQKKPN PPIKNEADNG LRNTRGTIAM ARTADKDSAT SQFFINVADN AFLDHGQRDF GYAVFGKVVK GMDVADKISQ VPTHDVGPYQ NVPSKPVVIL SAKVLP. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: 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 -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Reference: "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).