Western Blot: Factor Inhibiting HIF-1 Antibody (162c) [NBP1-30333] - Analysis in A431 cell lysates using NBP1-30333.
Immunocytochemistry/ Immunofluorescence: Factor Inhibiting HIF-1 Antibody (162c) [NBP1-30333] - FIH (162C) antibody was tested in A431 cells with FITC (green). Nuclei and alpha-tubulin were counterstained with Dapi ...read more
Immunohistochemistry: Factor Inhibiting HIF-1 Antibody (162c) [NBP1-30333] - Analysis of FIH in human renal cancer using DAB with hematoxylin counterstain.
This Factor Inhibiting HIF-1 antibody is useful for Immunocytochemistry/Immunofluorescence, Immunohistochemistry paraffin embedded sections and Western blot analysis where a band can be seen at 40 kDa. Prior to immunostaining paraffin tissues, antigen retrieval with sodium citrate buffer (pH 6.0) is recommended.
The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
40 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
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.
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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