FIH-1/HIF-1AN Antibody [FITC] Summary
Immunogen |
A synthetic peptide made to the C-terminal region of human Factor Inhibiting HIF-1 (between residues 300 and the C-terminus). [UniProt# Q9NWT6] |
Localization |
Nuclear |
Isotype |
IgG |
Clonality |
Polyclonal |
Host |
Rabbit |
Gene |
HIF1AN |
Purity |
Immunogen affinity purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Electron Microscopy
- Immunocytochemistry/ Immunofluorescence
- Immunohistochemistry
- Immunohistochemistry-Frozen
- Immunohistochemistry-Paraffin
- Immunoprecipitation
- Knockdown Validated
- Knockout Validated
- Western Blot
|
Application Notes |
Optimal dilution of this antibody should be experimentally determined. |
Reactivity Notes
Human, rat and mouse (PMID 19720742).
Packaging, Storage & Formulations
Storage |
Store at 4C in the dark. |
Buffer |
PBS |
Preservative |
0.05% Sodium Azide |
Purity |
Immunogen affinity purified |
Alternate Names for FIH-1/HIF-1AN Antibody [FITC]
Background
Factor inhibiting HIF1 (FIH1) is an asparaginyl hydroxylase enzyme that regulates HIF's transcriptional activity by hydroxylating HIF-1 alpha at 'Asp-803' in the CAD (C-terminal transactivation domain). Hydroxylation via PHDs followed by proteosome degradation is another mechanism that regulates HIF1, however, FIH1 is able to exercise the control even under severe hypoxic conditions, when PHD enzymes fail to do so. Localized mainly in cytoplasm, FIH1 functions as oxygen sensor and FIH1 interaction with NOTCH1 results in its nuclear localization whereas FIH1-ABPA3 interaction leads to its perinuclear localization. During normoxic conditions, FIH1 hydroxylates a conserved asparaginyl residue within CTAD of HIF-1 alpha/HIF-2 alpha, leading to steric clash that prevents the recruitment of the co-activators p300 and CBP. On the other hand, under hypoxic conditions, FIH1 is inactive, which results in activation of HIF-alpha signaling. FIH1 is involved in transcriptional repression through interaction with HIF1A, VHL and HDAC and hydroxylates specific Asn residues within ARD (ankyrin repeat domains) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A as well as other ARD-containing proteins. FIH1 also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. FIH1 has the ability to negatively regulate NOTCH1 activity thus accelerating myogenic differentiation, and positively regulates ASB4 activity which promotes vascular differentiation. FIH1-Mint3 binding affects FIH1's ability to modify HIF-1 alpha in an oxygen-independent manner and FIH1-Bax interaction plays inhibitory role in apoptosis.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are
guaranteed for 1 year from date of receipt.
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Secondary Antibodies
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