protein

Recombinant Human Dihydrofolate Reductase

MBS143726

0.01 mg

140 USD

Recombinant Protein

Recombinant Human Dihydrofolate Reductase

Dihydrofolate Reductase

DHFR Human; Dihydrofolate Reductase Human Recombinant; Dihydrofolate reductase; DHFR; DHFRP1

dihydrofolate reductase isoform 1; Dihydrofolate reductase; dihydrofolate reductase; dihydrofolate reductase

DHFR

DHFR; DHFR; DYR; DHFRP1

DYR_HUMAN

E Coli

187

MGSSHHHHHH SSGLVPRGSH MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND.

Greater than 95.0% as determined by SDS-PAGE.

The DHFR solution contains 20mM Tris-HCl buffer (pH8.0), 0.1M Nacl 2mM DTT, and 30% glycerol. Sterile Filtered colorless solution.

1 mg/ml

Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

Biological Activity: Specific activity is 1.5 - 2.5 units/ml and was obtained by measuring the oxidation of NADPH in absorbance at 340 nm during reaction. One unit will convert 1.0 umole of 7,8 dihydrofolate and beta-NADPH to 5,6,7,8-tetrahydrofolate and beta-NADP per minute at pH 6.5 at 25C.

ENZYMES; Enzymes; Reductase

Description: DHFR Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.6kDa.The DHFR is purified by proprietary chromatographic techniques. Introduction: Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes. DHFR deficiency is associated with megaloblastic anemia.DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid.DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.

4503323

NP_000782.1

NM_000791.3

P00374

15,672 Da

Cell Cycle Pathway (530733); Cell Cycle, Mitotic Pathway (105765); Defective AMN Causes Hereditary Megaloblastic Anemia 1 Pathway (906000); Defective BTD Causes Biotidinase Deficiency Pathway (906015); Defective CD320 Causes Methylmalonic Aciduria Pathway (906012); Defective CUBN Causes Hereditary Megaloblastic Anemia 1 Pathway (906001); Defective GIF Causes Intrinsic Factor Deficiency Pathway (906004); Defective HLCS Causes Multiple Carboxylase Deficiency Pathway (906014); Defective LMBRD1 Causes Methylmalonic Aciduria And Homocystinuria Type CblF Pathway (906003); Defective MMAA Causes Methylmalonic Aciduria Type CblA Pathway (906010)

Dihydrofolate reductase converts dihydrofolate into tetrahydrofolate, a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and certain amino acids. While the functional dihydrofolate reductase gene has been mapped to chromosome 5, multiple intronless processed pseudogenes or dihydrofolate reductase-like genes have been identified on separate chromosomes. Dihydrofolate reductase deficiency has been linked to megaloblastic anemia. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2014]

DHFR: Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFRL1. Defects in DHFR are the cause of megaloblastic anemia due to dihydrofolate reductase deficiency (DHFRD). DHFRD is an inborn error of metabolism, characterized by megaloblastic anemia and/or pancytopenia, severe cerebral folate deficiency, and cerebral tetrahydrobiopterin deficiency. Clinical features include variable neurologic symptoms, ranging from severe developmental delay and generalized seizures in infancy, to childhood absence epilepsy with learning difficulties, to lack of symptoms. Belongs to the dihydrofolate reductase family. Protein type: EC 1.5.1.3; Cofactor and Vitamin Metabolism - folate biosynthesis; Cofactor and Vitamin Metabolism - one carbon pool by folate; Oxidoreductase. Chromosomal Location of Human Ortholog: 5q14.1. Cellular Component: nucleoplasm; cytosol. Molecular Function: mRNA binding; dihydrofolate reductase activity; drug binding; NADP binding. Biological Process: tetrahydrofolate metabolic process; G1/S-specific transcription in mitotic cell cycle; tetrahydrofolate biosynthetic process; vitamin metabolic process; nucleotide biosynthetic process; regulation of nitric-oxide synthase activity; folic acid metabolic process; one-carbon compound metabolic process; mitotic cell cycle; response to methotrexate; glycine biosynthetic process; nitric oxide metabolic process; water-soluble vitamin metabolic process; G1/S transition of mitotic cell cycle. Disease: Megaloblastic Anemia Due To Dihydrofolate Reductase Deficiency

0.01 mg

140 USD

0.05 mg

205

1 mg

1790