Thymidine Phosphorylase, Recombinant from Escherichia coli

CAT:
952-B2019685
Size:
5000 Units
  • Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
  • Dry Ice Shipment: No
Thymidine Phosphorylase, Recombinant from Escherichia coli - image 1

Thymidine Phosphorylase, Recombinant from Escherichia coli

  • Description:

    Thymidine Phosphorylase, Recombinant from Escherichia coli_x000D_ Catalog number: B2019685_x000D_ Lot number: Batch Dependent_x000D_ Expiration Date: Batch dependent_x000D_ Amount: 5000 units_x000D_ Molecular Weight or Concentration: N/A_x000D_ Supplied as: Solution_x000D_ Applications: a molecular tool for various biochemical applications_x000D_ Storage: 2-8°C_x000D_ Keywords: Thymidine:orthophosphate deoxy-D-ribosyltransferase_x000D_ 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._x000D_ _x000D_ References:_x000D_ 1: 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._x000D_ 2: Gbaj A, Edwards PN, Reigan P, Freeman S, Jaffar M, Douglas KT. Thymidine phosphorylase from Escherichia coli: tight-binding inhibitors as enzyme active-site titrants J Enzyme Inhib Med Chem. 2006 Feb;21(1):69-73._x000D_ 3: Karamitros CS, Somody CM, Agnello G, Rowlinson S. Engineering of the Recombinant Expression and PEGylation Efficiency of the Therapeutic Enzyme Human Thymidine Phosphorylase Front Bioeng Biotechnol. 2021 Dec 17;9:793985._x000D_ 4: Moghaddam A, Bicknell R. Expression of platelet-derived endothelial cell growth factor in Escherichia coli and confirmation of its thymidine phosphorylase activity Biochemistry. 1992 Dec 8;31(48):12141-6._x000D_ 5: Ding Q, Ou L, Wei D, Wei X. Optimum induction of recombinant thymidine phosphorylase and its application Nucleosides Nucleotides Nucleic Acids. 2011 May;30(5):360-8._x000D_ 6: Carlson CA, Stewart GJ, Ingraham JL. Thymidine salvage in Pseudomonas stutzeri and Pseudomonas aeruginosa provided by heterologous expression of Escherichia coli thymidine kinase gene J Bacteriol. 1985 Jul;163(1):291-5._x000D_ 7: Moskaleva ND, Sukhodolets VV. [Escherichia coli K-12 mutants for the thymidine phosphorylase structural gene that retain the anabolic function of the enzyme] Genetika. 1981;17(9):1606-17._x000D_ 8: McNally VA, Gbaj A, Douglas KT, Stratford IJ, Jaffar M, Freeman S, Bryce RA. Identification of a novel class of inhibitor of human and Escherichia coli thymidine phosphorylase by in silico screening Bioorg Med Chem Lett. 2003 Nov 3;13(21):3705-9._x000D_ 9: Esipov RS, Gurevich AI, Chuvikovsky DV, Chupova LA, Muravyova TI, Miroshnikov AI. Overexpression of Escherichia coli genes encoding nucleoside phosphorylases in the pET/Bl21(DE3) system yields active recombinant enzymes Protein Expr Purif. 2002 Feb;24(1):56-60._x000D_ 10: Levene M, Pacitti D, Gasson C, Hall J, Sellos-Moura M, Bax BE. Validation of an Immunoassay for Anti-thymidine Phosphorylase Antibodies in Patients with MNGIE Treated with Enzyme Replacement Therapy Mol Ther Methods Clin Dev. 2018 Aug 28;11:1-8. _x000D_ _x000D_ Products Related to Thymidine Phosphorylase, Recombinant from Escherichia coli can be found at Proteins
  • Short Description:

    Catalog Number: B2019685 (5000 units)_x000D_ Thymidine Phosphorylase (TP) is an enzyme that catalyzes the reversible phosphorolysis of thymidine to thymine and ribose-1-phosphate. It plays a crucial role in nucleotide metabolism and recycling of thymidine, essential for DNA synthesis and repair. The enzyme is produced using recombinant DNA technology in Escherichia coli. 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._x000D_ _x000D_
  • Weight:

    0.15
  • Length:

    2
  • Width:

    0.5
  • Height :

    0.5
  • CAS Number:

    9000-83-3