37294
Dihydrofolate Reductase from bovine liver
~8 U/mL, ammonium sulfate suspension, off-white
Synonyme(s) :
Tetrahydrofolate Dehydrogenase
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
bovine liver
Forme
ammonium sulfate suspension
Activité spécifique
≥6 U/mg protein
Concentration
~8 U/mL
Couleur
off-white
Densité
1.2 g/mL at 20 °C
Température de stockage
2-8°C
Application
Dihydrofolate reductase (DHFR) is involved in the synthesis of purines, thymidine and glycine in folate metabolism. DHFR, from bovine liver, is used for methotrexate analysis . DHFR is useful to study various cancers such as sarcomas, leukemias and head and neck cancers .
Actions biochimiques/physiologiques
Dihydrofolate reductase (DHFR) reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as an electron donor. The binding of antitumor agents, such as methotrexate, to DHFR prevents the formation of reduced folates, which are essential for DNA synthesis .
Définition de l'unité
1 U corresponds to the amount of enzyme which converts 1 μmol 7,8-dihydrofolate and NADPH to 5,6,7,8-tetrahydrofolate and NADP per minute at pH 6.5 and 25 °C
Forme physique
Suspension in 3.6 M ammonium sulfate solution, pH 7.0
Autres remarques
In folate metabolism for the synthesis of purines, thymidine and glycine
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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves
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H B Eastman et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(19), 8572-8576 (1991-10-01)
Dihydrofolate reductase (DHFR; EC 1.5.1.3) is required in folate metabolism for the synthesis of purines, thymidine, and glycine. Although there have been several reports of induction of DHFR enzyme by methotrexate (MTX), a drug that competitively inhibits DHFR, there are
Use of dihydrofolate reductase from bovine liver, rather than from L. casei, for determining methotrexate.
R J Brooks
Clinical chemistry, 24(3), 518-519 (1978-03-01)
Tetsuo Shimizu et al.
Anticancer research, 32(10), 4589-4596 (2012-10-13)
Pemetrexed inhibits three key folate enzymes: thymidylate synthetase (TYMS), dihydrofolate reductase (DHFR), and glycinamide ribonucleotide formyltransferase (GARFT). The relationship between the clinical efficacy of pemetrexed and the expression of folate enzymes in lung cancer cells is unknown. The purpose of
Luca Belmonte et al.
Critical reviews in eukaryotic gene expression, 22(3), 219-232 (2012-11-13)
A state-of-the-art review of the role of the Langmuir-Blodgett nanotemplate on protein crystal structures is here presented. Crystals grown by nanostructured template appear more radiation resistant than the classical ones, even in the presence of a third-generation highly focused beam
S P Chumakov et al.
Molekuliarnaia biologiia, 46(5), 699-711 (2012-11-20)
Association and degradation of protein complexes play essential role in a majority of normal and pathologic processes, which take place in living cell. Studying the underlying mechanisms of those interactions would give deeper understanding of specific causes of disease progression
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
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