Recombinant Human Uridine Phosphorylase 1 protein
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Recombinant Human Uridine Phosphorylase 1 protein is a Human Full Length protein, in the 1 to 173 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
UP, UPP1, Uridine phosphorylase 1, UPase 1, UrdPase 1
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Uridine Phosphorylase 1 plays an important role in the salvage pathway that maintains nucleotide homeostasis. This process is essential for the efficient recycling of nucleotides which supports DNA and RNA synthesis especially under conditions of limited de novo synthesis. UPP1 does not function as part of a larger enzyme complex operating independently for its specific biochemical activity. The enzyme helps maintain an adequate supply of uracil and cytosine which are important for many cellular processes including cell growth and division.
Pathways
Uridine Phosphorylase 1 is significantly involved in the pyrimidine salvage pathway and is also interconnected with the broader nucleotide metabolism pathway. These pathways are essential for the recycling and synthesis of nucleotides required for nucleic acid production. UPP1 works closely with thymidine phosphorylase (TYMP) and uridine-cytidine kinase both of which are vital in maintaining cellular nucleotide balance. These interactions between enzymes help ensure that cells have the necessary components for vital functions like DNA replication and repair.
Specifications
Form
Liquid
Additional notes
ab172847 is greater than 95% pure, as determined by SEC-HPLC and reducing SDS-PAGE. It is supplied as an 0.2 µM filtered solution.
General info
Function
Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate which can then be utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (PubMed : 7488099). Shows broad substrate specificity and can also accept deoxyuridine and other analogous compounds (Probable).
Sequence similarities
Belongs to the PNP/UDP phosphorylase family.
Target data
Product promise
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