Recombinant Human RPE Protein (His Tag)

The "ribulose phosphate binding" superfamily defined by the Structural Classification of Proteins (SCOP) database is considered the result of divergent evolution from a common (beta/alpha) (8) -barrel ancestor. The superfamily includes d-ribulose 5-phosphate 3-epimerase (RPE) ; orotidine 5'-monophosphate decarboxylase (OMPDC) ; and 3-keto-l-gulonate 6-phosphate decarboxylase (KGPDC) . Replication of the human genome requires the activation of thousands of replicons distributed along each one of the chromosomes. Each replicon contains an initiation; or origin; site; at which DNA synthesis begins. In enzymology; a L-ribulose-5-phosphate 3-epimerase is an enzyme that catalyzes the chemical reaction L-ribulose 5-phosphate to L-xylulose 5-phosphate. Hence; RPE has one substrate; L-ribulose 5-phosphate; and one product; L-xylulose 5-phosphate. RPE belongs to the family of isomerases; specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is L-ribulose-5-phosphate 3-epimerase. Other names in common use include L-xylulose 5-phosphate 3-epimerase; UlaE; and SgaU.

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.