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% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
M Q R K L K V T S L E P G T V V I T E Q A V D T C F K A E F E Q I V L G K R V I R K T D L N K K L V Q E L L L C S A E L S E F T T V V G N T M C T L D F Y E G Q G R L D G A L C S Y T E K D K Q A Y L E A A Y A A G V R N I E M E S S V F A A M C S A C G L Q A A V V C V T L L N R L E G D Q I S S P R N V L S E Y Q Q R P Q R L V S Y F I K K K L S K A
| Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
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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).
UP, UPP1, Uridine phosphorylase 1, UPase 1, UrdPase 1
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% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 8
Constituents: 1.17% Sodium chloride, 0.24% Tris, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
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.
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).
Belongs to the PNP/UDP phosphorylase family.
Uridine Phosphorylase 1 (UPP1) also known as UPase is a pyrimidine-nucleoside phosphorylase enzyme with a molecular mass of approximately 34 kDa. The enzyme catalyzes the reversible phosphorolysis of uridine and 2'-deoxyuridine to uracil and ribose 1-phosphate or deoxyribose 1-phosphate. This reaction is an important step in the pyrimidine salvage pathway where it contributes to nucleotide pool balance. UPP1 is expressed in a variety of tissues including liver kidney and colon reflecting its diverse physiological roles.
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.
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.
Uridine Phosphorylase 1 has been linked to cancer and metabolic disorders. Overexpression of UPP1 is often observed in particular cancers including colorectal cancer where its activity may contribute to cancer progression. In cancer UPP1 shows interaction with proteins like thymidine phosphorylase (TYMP) which is also overexpressed and enhances angiogenesis and tumor growth. Additionally altered UPP1 activity impacts pyrimidine metabolism which can lead to metabolic disorders that disrupt nucleotide balance further linking it to pathological states.
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