RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.
Background References
1. Samaniego F. et. al. Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2. Structure, function, and post-translational regulation. J. Biol. Chem. 269:30904-30910(1994).
Western blot analysis of IREB2 on different lysates with Mouse anti-IREB2 antibody (HA601271) at 1/2,000 dilution.
Lane 1: Jurkat cell lysate (20 µg/Lane) Lane 2: A549 cell lysate (20 µg/Lane) Lane 3: Mouse liver tissue lysate (40 µg/Lane) Lane 4: Mouse kidney tissue lysate (40 µg/Lane) Lane 5: Mouse heart tissue lysate (40 µg/Lane) Lane 6: Rat liver tissue lysate (40 µg/Lane)
Predicted band size: 105 kDa Observed band size: 105 kDa
Exposure time: 25 seconds;
4-20% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (HA601271) at 1/2,000 dilution was used in 5% NFDM/TBST at 4℃ overnight. Anti-Mouse IgG for IP, AlpSdAbs® VHH(HRP) (001-100-005) at 1/5,000 dilution was used for 1 hour at room temperature.
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