Recombinant Human DHFR Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8456-DR

R&D Systems, part of Bio-Techne
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8456-DR-100
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Key Product Details

Source

E. coli

Accession #

P00374

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Dihydrofolate Reductase/DHFR Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human Dihydrofolate Reductase/DHFR protein
Met1-Asp187, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Met1 & Val2

Predicted Molecular Mass

22 kDa

SDS-PAGE

23 kDa, reducing conditions

Activity

Measured by the reduction of dihydrofolic acid (DHF).
The specific activity is >5,500 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

8456-DR
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl, Glycerol, Brij-35 and DTT.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.

Background: Dihydrofolate Reductase/DHFR

Dihydrofolate Reductase (DHFR) is an approximately 21 kDa enzyme that catalyzes the NADPH-dependent reduction of dihydrofolate to tetrahydrofolate, which is crucial for the synthesis of purines, thymidylate, and certain amino acids (1-4). Structurally, DHFR consists of an eight-stranded beta-sheet and four alpha-helices (2). Human DHFR shares 90% amino acid identity with mouse and rat DHFR. In addition to acting as a cofactor, NADPH protects DHFR from degradation in vitro and in a cellular context (5-8). DHFR protein binds to its own mRNA to self-regulate translation (9-12). The enzymatic activity and subcellular localization of DHFR are at least partially regulated by post-translational modification. Mono-ubiquitination of DHFR by MDM2 reduces the activity of DHFR (13). DHFR is primarily cytoplasmic, but it has been shown to translocate to the nucleus in a SUMO-dependent manner (14). Due to its role in nucleotide biosynthesis, DHFR has long been a therapeutic target for the treatment of various cancers and infectious diseases (15, 16).

References

  1. Bertino, J.R. et al. (1965) Biochemistry 4:839.
  2. Schweitzer, B.I. et al. (1990) FASEB J. 4:2441.
  3. Fierke, C.A. et al. (1987) Biochemistry 26:4085.
  4. Abali, E.E. et al. (2008) Vitam. Horm. 79:267.
  5. Perkins, J.P. et al. (1967) J. Biol. Chem. 242:4771.
  6. Wallace, L.A. and C. Robert Matthews (2002) J. Mol. Biol. 315:193.
  7. Ainavarapu, S.R. et al. (2005) Biophys. J. 89:3337.
  8. Hsieh, Y.C. et al. (2013) Mol. Pharmacol. 83:339.
  9. Chu, E. et al. (1993) Biochemistry 32:4756.
  10. Ercikan, E. et al. (1993) Adv. Exp. Med. Biol. 338:537.
  11. Ercikan-Abali, E.A. et al. (1997) Biochemistry 36:12317.
  12. Tai, N. et al. (2004) Biochem. J. 378:999.
  13. Maguire, M. et al. (2008) Cancer Res. 68:3232.
  14. Anderson, D.D. et al. (2007) Clin. Chem. Lab. Med. 45:1760.
  15. Goldman, I.D. et al. (2010) Curr. Opin. Investig. Drugs 11:1409.
  16. Sharma, M. and P.M. Chauhan (2012) Future Med. Chem. 4:1335.

Alternate Names

DHFR, DHFRP1, DYR

Entrez Gene IDs

1719 (Human); 13361 (Mouse); 24312 (Rat)

Gene Symbol

DHFR

UniProt

P00374 (Human)

Additional Dihydrofolate Reductase/DHFR Products

Product Documents for Recombinant Human DHFR Protein, CF

Product Datasheets

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Product Specific Notices for Recombinant Human DHFR Protein, CF

For research use only

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