epitope mapping near the N-terminus of FIH-1 of human origin
recommended for detection of FIH-1 of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, canine and porcine
FIH-1 Background Information Factor inhibiting HIF-1 (FIH-1) exists as a homodimer and binds to HIF-1å. Specifically, FIH-1 operates as an asparaginyl hydroxylase. It catalyzes the hydroxylation of the ∫-carbon of Asparagine residue 803 within the carboxy terminal transactivation domain of HIF-1å. This hydroxylation event blocks the association of HIF-1å with co-activators. FIH-1 also binds to von Hippel-Lindau (VHL) tumor suppressor protein, which represses transcriptional ac-tivity of HIF-1å. In transiently transfected human osteosarcoma cells, FIH-1 localizes to the cytoplasm. The structure of FIH-1 includes a jellyroll-like ∫-barrel containing ferrous-binding triad residues. The gene encoding human FIH-1 maps to chromosome 10q24.
FIH-1 (N-18) Product Citations
See how others have used FIH-1 (N-18): sc-26219 antibody and or FIH-1 (N-18) antibody conjugates.
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FIH-1 (N-18)
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FIH-1 (N-18): sc-26219. Western blot analysis of FIH-1 expression in Sol8 nuclear extract (A) and rat skeletal muscle tissue extract (B).
FIH-1 (N-18): sc-26219. Western blot analysis of FIH-1 expression in non-transfected: sc-117752 (A) and human FIH-1 transfected: sc-159159 (B) 293T whole cell lysates.
