epitope corresponding to amino acids 15-243 mapping within an internal region of FIH-1 of human origin
Modification Notes
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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
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, bovine and porcine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 15-243 mapping within an internal region of FIH-1 of human origin
Tissue Specificity
epitope corresponding to amino acids 15-243 mapping within an internal region 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, bovine and porcine:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.