抗FIH-1/HIF-1AN抗体 | Anti-FIH-1/HIF-1AN Antibody

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価格

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Image

	Western Blot: FIH-1/HIF-1AN Antibody [NB100-428] - Analysis of astrocytes lysate from Rat brain using FIH-1/HIF-1AN antibody at 1:500 dilution with ECL detection. The antibody detected a major band at ~40 kDa position representing FIH-1/HIF-1AN protein.
	Immunohistochemistry: FIH-1/HIF-1AN Antibody [NB100-428] - Detection of FIH-1 in rat brain tissue.

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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.

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