UMPS Human, Sf9
Sf9, Baculovirus cells.
Uridine Monophosphate Synthetase, UMP Synthase, Orotate Phosphoribosyl Transferase And Orotidine-5-Decarboxylase, Orotidine 5-Phosphate Decarboxylase, Orotate Phosphoribosyltransferase, Uridine 5-Monophosphate Synthase, OMPdecase, OPRTase, OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase, Orotidine 5'-phosphate decarboxylase, ODC.
Greater than 95.0% as determined by SDS-PAGE.
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Description
UMPS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 486 amino acids (1-480 a.a.) and having a molecular mass of 53kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). UMPS is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Uridine Monophosphate Synthetase, UMP Synthase, Orotate Phosphoribosyl Transferase And Orotidine-5-Decarboxylase, Orotidine 5-Phosphate Decarboxylase, Orotate Phosphoribosyltransferase, Uridine 5-Monophosphate Synthase, OMPdecase, OPRTase, OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase, Orotidine 5'-phosphate decarboxylase, ODC.
Sf9, Baculovirus cells.
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 HHHHHH.
Product Science Overview
UMPS is a bifunctional enzyme that combines two distinct enzymatic activities:
- Orotate Phosphoribosyltransferase (OPRTase): This activity catalyzes the conversion of orotate to orotidine-5’-monophosphate (OMP).
- Orotidine-5’-Monophosphate Decarboxylase (OMPdecase): This activity converts OMP to uridine-5’-monophosphate (UMP).
In eukaryotes, these two activities are linked into a single protein, which helps stabilize the catalytic centers and ensures efficient functioning of the enzyme .
The human recombinant UMPS produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 486 amino acids. It has a molecular mass of approximately 53 kDa . The enzyme is expressed with a 6-amino acid His tag at the C-terminus, which facilitates its purification using chromatographic techniques .
Recombinant UMPS is used in various research applications, including:
- Studying Pyrimidine Metabolism: Understanding the role of UMPS in pyrimidine biosynthesis can provide insights into cellular metabolism and the regulation of nucleotide synthesis.
- Disease Research: Mutations in the UMPS gene can lead to inherited orotic aciduria, a rare metabolic disorder. Studying recombinant UMPS can help researchers understand the molecular basis of this disease and develop potential treatments .
- Biotechnological Applications: Recombinant enzymes like UMPS are used in the production of nucleotides and nucleotide analogs, which have applications in pharmaceuticals and biotechnology.
