T6632
Thymidine Phosphorylase, recombinant from Escherichia coli
recombinant, expressed in E. coli, buffered aqueous solution, ≥900 units/mL, 0.2 μm filtered
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Synonym(s):
Thymidine:orthophosphate deoxy-D-ribosyltransferase
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
recombinant
expressed in E. coli
Quality Level
sterility
0.2 μm filtered
form
buffered aqueous solution
concentration
≥900 units/mL
UniProt accession no.
storage temp.
2-8°C
Gene Information
Escherichia coli K12 ... deoA(948901)
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General description
Thymidine phosphorylase inhibits vascular smooth muscle cell proliferation.
Application
Thymidine phosphorylase has been used in a study to evaluate biomarkers for advanced breast cancer patients treated with capecitabine-based first-line chemotherapy. Thymidine phosphorylase has also been used in a study to investigate implications for the clinical efficacy of nucleoside analogues.
Biochem/physiol Actions
An enzyme that catalyzes the reversible conversion of thymidine to thymine. Thymidine phosphorylase is part of the pyrimidine nucleoside salvage pathway. This pathway allows pyrimidine bases to be recycled for nucleotide biosynthesis, while the pentose 1-phosphates are converted to intermediates of the pentose phosphate shunt and glycolysis. The E. coli thymidine phosphorylase shares 40% sequence homology with the human sequence, which has been found to be identical to the angiogenic agent platelet-derived endothelial growth factor. The purified E. coli enzyme has been shown to stimulate blood vessel growth in chick chorioallantoic membrane assays.
Unit Definition
One unit will convert 1.0 μmole each of thymidine and phosphate to thymine and 2-deoxyribose 1-phosphate per min at pH 7.4 at 25°C.
Physical form
Solution in 0.5 M potassium phosphate containing 2 mM uracil, 0.02% sodium azide and bovine serum albumin
Preparation Note
Cloned from E. coli and produced in overexpressing E. coli
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Agnieszka Zagórska et al.
Materials (Basel, Switzerland), 14(15) (2021-08-08)
Cancer represents one of the most serious health problems and the second leading cause of death around the world. Heterocycles, due to their prevalence in nature as well as their structural and chemical diversity, play an immensely important role in
Domenico Ribatti et al.
Expert opinion on therapeutic targets, 16(12), 1215-1225 (2012-09-18)
Several anti-angiogenic agents have been developed and some of them have been clinically applied in the tumor therapy. Anti-angiogenic therapy faces some hurdles: inherent or acquired resistance, increased invasiveness, and lack of biomarkers. Characterization of tumor endothelial markers may help
Hong-Yun Zhao et al.
Anti-cancer drugs, 23(5), 534-542 (2012-04-07)
The aim of the present study was to investigate the gene expression of biomarkers associated with the sensitivity to fluoropyrimidine and taxanes in recurrent/advanced breast cancer patients treated with first-line capecitabine chemotherapy. We evaluated the clinicopathological/prognostic significance of thymidylate synthase
Sohail Anjum Shahzad et al.
Bioorganic chemistry, 85, 209-220 (2019-01-12)
Thymidine phosphorylase (TP) is over expressed in several solid tumors and its inhibition can offer unique target suitable for drug discovery in cancer. A series of 1,2,4-triazoles 3a-3l has been synthesized in good yields and subsequently inhibitory potential of synthesized
Michelle Levene et al.
Toxicological sciences : an official journal of the Society of Toxicology, 131(1), 311-324 (2012-09-15)
Erythrocyte-encapsulated thymidine phosphorylase (EE-TP) is currently under development as an enzyme replacement therapy for mitochondrial neurogastrointestinal encephalomyopathy (MNGIE), an autosomal recessive disorder caused by a deficiency of thymidine phosphorylase. The rationale for the development of EE-TP is based on the
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