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Merck

37294

Dihydrofolate Reductase from bovine liver

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

Synonim(y):

Tetrahydrofolate Dehydrogenase

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Informacje o tej pozycji

Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
Numer WE:
MDL number:

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Nazwa produktu

Dihydrofolate Reductase from bovine liver, ~8 U/mL, ammonium sulfate suspension, off-white

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

Quality Level

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Ta pozycja
L2011M5257L7525
biological source

bovine liver

biological source

-

biological source

chicken liver

biological source

Porcine heart

specific activity

≥6 U/mg protein

specific activity

≥250 units/mg protein (biuret)

specific activity

10-30 units/mg protein (modified Warburg-Christian)

specific activity

≥200 units/mg protein

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

ammonium sulfate suspension

concentration

~8 U/mL

concentration

-

concentration

-

concentration

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

color

off-white

color

-

color

-

color

-

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 [1]. DHFR is useful to study various cancers such as sarcomas, leukemias and head and neck cancers [2].

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 [2].

Other Notes

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
In folate metabolism for the synthesis of purines, thymidine and glycine[3]
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Physical form

Suspension in 3.6 M ammonium sulfate solution, pH 7.0
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Klasa składowania

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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)
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
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
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

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