Rabbit HIF1AN Monoclonal Antibody | anti-Hif1an antibody

HIF1AN (Hypoxia Inducible Factor 1 alpha Inhibitor, DKFZp762F1811, Factor Inhibiting HIF1, FIH1, FLJ20615, FLJ22027, Hypoxia Inducible Factor Asparagine Hydroxylase, Prolyl Hydroxylase)

Cat. Num. AAA607056

• Gene Names: Hif1an; FIH1; 2310046M24Rik; A830014H24Rik
• Reactivity: Human, Monkey, Mouse, Rat
• Applications: Western Blot
• Synonyms: HIF1AN; Monoclonal Antibody; HIF1AN (Hypoxia Inducible Factor 1 alpha Inhibitor; DKFZp762F1811; Factor Inhibiting HIF1; FIH1; FLJ20615; FLJ22027; Hypoxia Inducible Factor Asparagine Hydroxylase; Prolyl Hydroxylase); Anti -HIF1AN (Hypoxia Inducible Factor 1 alpha Inhibitor; anti-Hif1an antibody

• Host: Rabbit
• Reactivity: Human, Monkey, Mouse, Rat
• Clonality: Monoclonal
• Isotype: IgG
• Clone Number: 10E26
• Specificity: Recognizes human FIH. Species crossreactivity: mouse, rat, monkey.
• Form/Format: Supplied in liquid 10mM sodium HEPES pH 7.5, 150mM NaCl, 100ug/ml BSA, 50% glycerol and 0.02% sodium azide.

• Applicable Applications for anti-Hif1an antibody: Western Blot (WB)
• Application Notes: Suitable for use in Western Blot.; Dilution: Western Blot: 1:1000. Incubate membrane with diluted antibody in 5% w/v BSA, 1X TBS, 0.1%; Tween-20 at 4 degree C with gentle shaking, overnight.
• Immunogen: Synthetic peptide corresponding to residues surrounding Tyr35 of human FIH protein (KLH-coupled).
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, aliquot and store at -20 degree C. Aliquots are stable for at least 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Western Blot (WB)

(Western blot analysis of extracts from various cell types using MBS607056.)

Related Product Information for anti-Hif1an antibody

FIH (Factor inhibiting HIF-1, HIF asparagine hydroxylase) is a dioxygen-dependent asparaginyl hydroxylase that modifies target protein function by hydroxylating target protein asparagine residues (1-3). Hypoxia-inducible factor (HIF), a transcriptional activator involved in control of cell cycle in response to hypoxic conditions, is an important target for FIH regulation. FIH functions as an oxygen sensor that regulates HIF function by hydroxylating at Asn803 in the carboxy-terminal transactivation domain (CAD) of HIF (4,5). During normoxia, FIH uses cellular oxygen to hydroxylate HIF-1 and prevent interaction of HIF-1 with transcriptional coactivators, including the CBP/p300-interacting transactivator. Under hypoxic conditions, FIH remains inactive and does not inhibit HIF, allowing the activator to regulate transcription of genes in response to low oxygen conditions (4-6). FIH activity is regulated in through interaction with proteins, including Siah-1, which targets FIH for proteasomal degradation (7). The Cut-like homeodomain protein CDP can bind the FIH promoter region to regulate FIH expression at the transcriptional level (8). Phosphorylation of HIF at Thr796 also can prevent FIH hydroxylation on Asn803 (9). Potential FIH substrates also include proteins with ankyrin repeat domains, such as I -B, Notch, and ASB4 (10-12).

Product Categories/Family for anti-Hif1an antibody

Antibodies; Abs to Transcription Factors

NCBI and Uniprot Product Information

• NCBI GI #: 70909332
• NCBI GeneID: 319594
• NCBI Accession #: NP_795932.2
• NCBI GenBank Nucleotide #: NM_176958.3
• UniProt Accession #: Q8BLR9; Q3U3G4; A1L3B7
• Molecular Weight: 40,241 Da
• NCBI Official Full Name: hypoxia-inducible factor 1-alpha inhibitor
• NCBI Official Synonym Full Names: hypoxia-inducible factor 1, alpha subunit inhibitor
• NCBI Official Symbol: Hif1an
• NCBI Official Synonym Symbols: FIH1; 2310046M24Rik; A830014H24Rik
• NCBI Protein Information: hypoxia-inducible factor 1-alpha inhibitor; hypoxia-inducible factor asparagine hydroxylase
• UniProt Protein Name: Hypoxia-inducible factor 1-alpha inhibitor
• Protein Family: Hypoxia-inducible factor 1-alpha inhibitor
• UniProt Gene Name: Hif1an
• UniProt Entry Name: HIF1N_MOUSE

Uniprot Description

HIF1AN: Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300- interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation. Homodimer; homodimerization is essential for catalytic activity. Interacts with VHL and HIF1A. Part of a complex with VHL, HIF1A and HDAC1 or HDAC2 or HDAC3. Interacts with NFKB1 and NFKBIA. Interacts with NOTCH1, NOTCH2 and NOTCH3 but not with NOTCH4. Interacts with APBA3; binding inhibits HIF1AN binding to HIF1A. Interacts with TNKS2. Interacts with PPP1R12A. Interacts with ASB4.

Protein type: EC 1.14.11.30; EC 1.14.11.n4; Oxidoreductase

Cellular Component: nucleoplasm; perinuclear region of cytoplasm; cytoplasm; nucleus

Molecular Function: NF-kappaB binding; protein homodimerization activity; dioxygenase activity; zinc ion binding; carboxylic acid binding; iron ion binding; metal ion binding; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; oxidoreductase activity; Notch binding; cofactor binding

Biological Process: peptidyl-aspartic acid hydroxylation; regulation of transcription, DNA-dependent; transcription, DNA-dependent; peptidyl-asparagine hydroxylation; negative regulation of Notch signaling pathway; positive regulation of myoblast differentiation