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E. coli Uridine Phosphorylase (UPase) Proteins Molecular Depot
E. coli Uridine Phosphorylase (UPase) Proteins Molecular Depot
E. coli Uridine Phosphorylase (UPase) Proteins Molecular Depot
E. coli Uridine Phosphorylase (UPase) Proteins Molecular Depot

E. coli Uridine Phosphorylase (UPase)

$907.00

    Catalog Number: B2015249 (10 ug)

    E. coli Uridine Phosphorylase (UPase) is a high quality E. coli Uridine Phosphorylase (UPase). This product has been used as a molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

    Products are for in vitro research use only (RUO).

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E. coli Uridine Phosphorylase (UPase) – Catalog Number: B2015249 (10 µg)

Catalog number: B2015249
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 10 µg
Molecular Weight or Concentration: 29.3 kDa
Supplied as: Solution
Applications: a molecular tool for various biochemical applications
Storage: -20 °C
Keywords: Udp, UrdPase
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

Scientific Description

E. coli Uridine Phosphorylase (UPase) (Catalog B2015249, 10 µg in solution, ~29.3 kDa) catalyzes the reversible phosphorolytic cleavage of uridine into uracil and α-D-ribose-1-phosphate in the presence of inorganic phosphate. This enzyme, also known as Udp or UrdPase, is a key player in pyrimidine metabolism, particularly in nucleotide salvage pathways :contentReference[oaicite:1]{index=1}.

Supplied in a biotechnology-grade solution and stored at –20 °C, this UPase offers excellent purity and stability, ideal for enzymological assays, pathway reconstruction, or metabolic labeling studies. Its defined molecular weight supports downstream analytical verification, while the solution format enables precise volume delivery and rapid integration into assay workflows.

Researchers commonly utilize this enzyme to trace uridine turnover, validate salvage pathway models, and study enzyme kinetics under varying substrate and cofactor conditions. Its activity supports both basic biochemical research and advanced applications such as substrate specificity assays or structural biology studies. The high purity and consistent format aid in reproducibility across collaborative labs and complex multi-step workflows.

Why researchers choose this product:

  • Defined amount (10 µg) and molecular weight (29.3 kDa) for dependable dosing and standardization
  • Efficient reversible conversion of uridine to uracil + ribose-1-phosphate, supporting pyrimidine salvage research
  • Biotechnology-grade solution ensures purity and ease of use in sensitive protocols
  • Solution format and –20 °C storage promote rapid deployment and long-term stability

This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use.

References

  • Komissarov AA, Debabov VG. Modification with tetranitromethane of an essential tyrosine residue in uridine phosphorylase from Escherichia coli Biochim Biophys Acta. 1995 Oct 25;1252(2):239-44.
  • Liu M, Cao D, Russell R, Handschumacher RE, Pizzorno G. Expression, characterization, and detection of human uridine phosphorylase and identification of variant uridine phosphorolytic activity in selected human tumors Cancer Res. 1998 Dec 1;58(23):5418-24.
  • Komissarov AA, Romanova DV, Dmitrieva NA, Linkova EV, Mironov AS, Debabov VG. Selective modification of putative uridine-binding site of uridine phosphorylase from E. coli with fluorescein 5′-isothiocyanate Biochim Biophys Acta. 1994 Mar 16;1205(1):54-8.
  • Tanabe T, Fukuzawa H, Amatatsu Y, Matsui K, Ohtsuka H, Maeda Y, Sato H. Identification of an antilymphocyte transformation substance from Pasteurella multocida Microbiol Immunol. 2019 Jul;63(7):261-268.
  • Morgunova EYu, Mikhailov AM, Popov AN, Blagova EV, Smirnova EA, Vainshtein BK, Mao C, Armstrong ShR, Ealick SE, Komissarov AA, et al. Atomic structure at 2.5 Å resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice FEBS Lett. 1995 Jun 26;367(2):183-7.
  • Takehara M, Ling F, Izawa S, Inoue Y, Kimura A. Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp Biosci Biotechnol Biochem. 1995 Oct;59(10):1987-90.
  • Chebotarev DV, Gul’ko LB, Veĭko VP. [Protein engineering of uridine phosphorylase from Escherichia coli K-12. II. Comparative study of hybrid and mutant forms of uridine phosphorylases] Bioorg Khim. 2001 May-Jun;27(3):184-90.
  • Obata H, Muryoi N, Kawahara H, Nishiyama A. Purification and characterization of uridine phosphorylase from the ice-nucleating bacterium, Pantoea agglomerans NBRC12686 Cryo Lett. 2004 May-Jun;25(3):195-204.
  • Molchan OK, Dmitrieva NA, Romanova DV, Lopes LE, Debabov VG, Mironov AS. Isolation and initial characterization of the uridine phosphorylase from Salmonella typhimurium Biochemistry (Mosc). 1998 Feb;63(2):195-9.
  • Ge C, OuYang L, Ding Q, Ou L. Co-expression of recombinant nucleoside phosphorylase from Escherichia coli and its application Appl Biochem Biotechnol. 2009 Oct;159(1):168-77.

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Product Resources:

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Copy of Technical Specifications

FeatureDetails
Viewing Head Siedentopf type trinocular head, inclined at 30°, Interpupillary adjustment 53mm to 75mm, graduated diopter on left eyetube (30mm I.D. eyetubes)
Eyepieces SWH10X Widefield high eyepoint eyepiece, Field No. 22, tube O.D. 30.0 mm
Nosepiece Quintuple
Quintuple LWD Planachromat Phase 10x, 20x
Condenser TC Condenser N.A. 0.30, W.D. 73.0mm
Stage180mm(X) x 245mm(Y) plain stage with replaceable glass insert with 45mm opening, Glass Stage plate insert
IlluminationKoehler without iris, with phase slider, 3W LED
WarrantyLIMITED LIFETIME WARRANTY

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