UPP1 Human
Description
UPP1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Product Specs
CSNVTIIRIG TSGGIGLEPG TVVITEQAVD TCFKAEFEQI VLGKRVIRKT DLNKKLVQEL LLCSAELSEF TTVVGNTMCT LDFYEGQGRL DGALCSYTEK DKQAYLEAAY AAGVRNIEME SSVFAAMCSA CGLQAAVVCV TLLNRLEGDQ
ISSPRNVLSE YQQRPQRLVS YFIKKKLSKA.
Product Science Overview
Uridine Phosphorylase 1 (UPP1) is a critical enzyme involved in the pyrimidine salvage pathway, which is essential for maintaining uridine homeostasis in the body. This enzyme catalyzes the reversible phosphorolysis of uridine to uracil and ribose-1-phosphate . The human recombinant form of UPP1 has been extensively studied due to its significant role in various biochemical processes and its potential therapeutic applications.
UPP1 belongs to the family of pentosyltransferases and is expressed in the cytosol of most tissues . It is particularly abundant in certain tumors, where it plays a crucial role in the activation of pyrimidine nucleoside analogues used in chemotherapy, such as 5-fluorouracil (5-FU) and its prodrug, capecitabine . The enzyme’s ability to catalyze the conversion of uridine to uracil and ribose-1-phosphate is vital for the salvage of pyrimidine nucleotides, which are necessary for DNA and RNA synthesis .
Recombinant human UPP1 is typically produced using Escherichia coli (E. coli) as the expression system. The gene encoding UPP1 is cloned into an appropriate expression vector, which is then introduced into E. coli cells. The recombinant protein is expressed with an N-terminal His-tag to facilitate purification. After expression, the cells are lysed, and the protein is purified using affinity chromatography techniques . The purified protein is then subjected to various assays to confirm its activity and purity.
The primary reaction catalyzed by UPP1 is the reversible phosphorolysis of uridine to uracil and ribose-1-phosphate . This reaction is crucial for the pyrimidine salvage pathway, allowing cells to recycle uridine and maintain nucleotide pools. Additionally, UPP1 plays a significant role in the activation of chemotherapeutic agents. For example, it converts 5-FU to 5-fluorouridine, which is further phosphorylated to its active form by uridine kinase .
The elevated expression of UPP1 in certain tumors has made it a target for cancer therapy. Inhibitors of UPP1, such as 5-benzylacyclouridine (BAU), have been developed to modulate the cytotoxic side effects of 5-FU and its derivatives . By inhibiting UPP1, these compounds can increase the therapeutic index of chemotherapeutic agents, selectively protecting normal tissues with lower UPP1 activity .
