pDRIVE-CMV / FerL / chEF1

CMV / FerL / chEF1 promoter (Ubiquitous) in pDRIVE expression plasmid

CMV enh / Ferritin L prom / EF-1α 5’UTR 

Ferritin is a ubiquitous iron storage protein, whose major role is to sequester and detoxify intracellular iron that has not been utilized in cellular metabolism.

Ferritin is a 24 subunit protein composed of two subunit types, termed H (heavy) and L (light), which perform complementary functions in the protein.

The H subunit plays a role in the rapid detoxification of iron whereas the L subunit facilitates long-term iron storage.

The synthesis of ferritin is highly regulated by the iron status of the cell. The iron regulation is achieved at the translational level through interaction between a 28-nucleotide iron-responsive element (IRE), located in the 5’ untranslated region (5’UTR) of ferritin mRNAs, and a cytosolic protein, the iron regulatory protein [1].

To eliminate the iron regulation of the ferritin promoters, the 5’UTR of FerH and FerL have been replaced by the 5’UTR of the HTLV or EF-1α.

References:

1. Eisenstein RS & Munro HN. 1990. Translational regulation of ferritin synthesis by iron. Enzyme 44(1-4):42-58.
2. Bevilacqua MA et al. 1992. Promoter for the human ferritin heavy chain-encoding gene (FERH): structural and functional characterization. Gene 15;111(2):255-60.