E.coli udp protein (Recombinant) (His-Tag) (STJP016801)

SPECIFICATIONS
HostE.coli
ImmunogenE.coli
STJP016801
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General Information

Short DescriptionRecombinant-E.coli udp-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications.
ApplicationsSDS-PAGE/Enzyme Activity
HostE.coli
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

Concentration1 mg/mL
FormulationLiquid in 20mM Tris-HCl buffer (pH 8.0) containing 10% Glycerol, 1mM DTT, 50mM NaCl
Storage InstructionFor short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles.
ImmunoreactivitySpecific activity is > 20, 000pmol/min/ug, and is defined as the amount of enzyme that catalyze the reduction 1.0pmole of uridine presence of phosphate per minute at pH 7.5 at 25C.

Target Information

Accession NumberNP_418275
ImmunogenE.coli
Immunogen Region1-253aa
Immunogen Sequence MSKSDVFHLG LTKNDLQGAT LAIVPGDPDR VEKIAALMDK PVKLASHREF TTWRAELDGK PVIVCSTGIG GPSTSIAVEE LAQLGIRTFL RIGTTGAIQP HINVGDVLVT TASVRLDGAS LHFAPLEFPA VADFECTTAL VEAAKSIGAT THVGVTASSD TFYPGQERYD TYSGRVVRHF KGSMEEWQAM GVMNYEMESA TLLTMC

Additional Info

Background uridine phosphorypase (uDP) catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose-or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is uridine:phosphate alpha-D-ribosyltransferase. Other names in common use include pyrimidine phosphorylase, urdPase, uPH, and uPase. Recombinant E. coli uDP protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.

Information sourced from Uniprot.org

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