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.
A DNA sequence encoding the human RPE isoform 1 (NP_954699.1) (Ala 2-Arg 228) was expressed; with a polyhistidine tag at the N-terminus.
Purity:
> 94 % as determined by reducing SDS-PAGE.
Mol Mass:
27 kDa
AP Mol Mass:
30 kDa
Formulation:
Lyophilized from sterile 50mM Tris; 100mM NaCl; pH 8.0
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
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.