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MilliporeSigma

37294

Sigma-Aldrich

Dihydrofolate Reductase from bovine liver

~8 U/mL, ammonium sulfate suspension, off-white

Sinónimos:

Tetrahydrofolate Dehydrogenase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine liver

form

ammonium sulfate suspension

specific activity

≥6 U/mg protein

concentration

~8 U/mL

color

off-white

density

1.2 g/mL at 20 °C

storage temp.

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 .

Biochem/physiol Actions

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 .

Unit Definition

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

Physical form

Suspension in 3.6 M ammonium sulfate solution, pH 7.0

Other Notes

In folate metabolism for the synthesis of purines, thymidine and glycine
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Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


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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)
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
Shimon Bershtein et al.
Molecular cell, 49(1), 133-144 (2012-12-12)
What are the molecular properties of proteins that fall on the radar of protein quality control (PQC)? Here we mutate the E. coli's gene encoding dihydrofolate reductase (DHFR) and replace it with bacterial orthologous genes to determine how components of PQC
Inbar Avraham et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(52), E3678-E3686 (2012-12-01)
Plasmodium falciparum causes the deadliest form of human malaria. Its virulence is attributed to its ability to modify the infected RBC and to evade human immune attack through antigenic variation. Antigenic variation is achieved through tight regulation of antigenic switches
Luca Freschi et al.
Molecular bioSystems, 9(1), 36-43 (2012-10-27)
One of the most important challenges in systems biology is to understand how cells respond to genetic and environmental perturbations. Here we show that the yeast DHFR-PCA, coupled with high-resolution growth profiling (DHFR-qPCA), is a straightforward assay to study the

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