Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2′-deoxycytidine for UMP synthesis. This protein is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as arabinofuranosyl cytidine (Ara-C) and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function.
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Cytidine deaminase (CDA) is mainly expressed in granulocytes and can form homotetramers. Recombinant human CDA protein, fused to His-tag at N-terminus, was expressed in Escherichia coli and purified by using conventional chromatography.
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0.5 mg/mL in 20 mM Tris-HCl buffer (pH 8.0) containing 100 mM NaCl, 1 mM DTT, 2 mM EDTA and 40% glycerol.
Ultrasound in medicine & biology, 47(6), 1596-1615 (2021-03-13)
In this study we compared three different microbubble-based approaches to the delivery of a widely used chemotherapy drug, gemcitabine: (i) co-administration of gemcitabine and microbubbles (Gem+MB); (ii) conjugates of microbubbles and gemcitabine-loaded liposomes (GemlipoMB); and (iii) microbubbles with gemcitabine directly
Highly specific and potent inhibitors of dihydroorotate dehydrogenase (DHODH), an essential enzyme of the de novo pyrimidine ribonucleotide synthesis pathway, are in clinical trials for autoimmune diseases, viral infections and cancer. However, because DHODH inhibitors (DHODHi) are immunosuppressants they may
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