Recombinant humaan UMPS-eiwit

Uridine 5'-monophosphate synthase, also known as UMPS, is a bifunctional enzyme that catalyzes the final two steps of the de novo pyrimidine biosynthetic pathway. unlike prokaryotes, UMPS in eukaryotes combines the orotate phosphoribosyltransferase and the orotidine-5'-monophosphate (OMP) decarboxylase activities into a single protein. The union of these two enzymes is thought to stabilize the catalytic centers due to the low molar concentration of the protein in mammalian cells. Defects in this gene are the cause of hereditary orotic aciduria. Recombinant human UMPS protein, fused to His-tag at N-terminus, was expressed in E. coli.

Uridine 5'-monophosphate synthase, OPRT

E.coli

Human

His-Tag

SDS-PAGE, Denatured

1 mg/mL (determined by Bradford assay)

> 85% by SDS-PAGE

54.3 kDa (500aa)

UMPS, uridine 5'-monophosphate synthase, OPRT, ATGP1788-10 µg, ATGP1788-20 µg, ATGP1788-50 µg, ATGP1788-100 µg, ATGP1788-250 µg, ATGP1788-500 µg, ATGP1788-1 mg, ATGP1788-10, ATGP1788-20, ATGP1788-50, ATGP1788-100, ATGP1788-250, ATGP1788-500, ATGP1788-1

Suchi M., et al. (1997) Genet. 60:525-539.; ; Yablonski M J., et al. (1996) J Biol Chem. 271:10704-10708.;

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 2M urea, 20% glycerol

Metabolism

NP_000364

P11172

Human

MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV