|Calculated MW||23.6 kDa (207 aa, 1-187 aa + NT His-Tag)|
|Other Names||Dihydrofolate reductase.|
|Results||1.5 - 2.5 units/ml|
|Sequence||MGSSHHHHHH SSGLVPRGSH MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND|
|Storage||-80°C; 1 mg/ml solution in 20 mM Tris-HCl buffer (pH 8.0) containing 0.1 M NaCl, 2 mM DTT and 30% glycerol.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
DHFR, also known as Dihydrofolate reductase, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to tetrahydrofolate cofactors used in 1-carbon transfer chemistry. Dihydrofolate reductase deficiency has been linked to megaloblastic anemia. Human dihydrofolate reductase has been used in a study to investigate the stable expression of green fluorescent protein and the targeted disruption of thioredoxin peroxidase-1 gene in Babesia bovis. Human dihydrofolate reductase has also been used in a study to investigate the structural analysis of human dihydrofolate reductase as a binary complex.
Chen M.-J.,et al.J. Biol. Chem. 259:3933-3943(1984).
Masters J.N.,et al.Gene 21:59-63(1983).
Yang J.K.,et al.J. Mol. Biol. 176:169-187(1984).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Schmutz J.,et al.Nature 431:268-274(2004).
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