Porcine Hypoxia Inducible Factor 1 Alpha (HIF1a) ELISA Kit | HIF1a elisa kit

Porcine Hypoxia Inducible Factor 1 Alpha (HIF1a) ELISA Kit

Cat. Num. AAA9307260

• Reactivity: Porcine
• Synonyms: Hypoxia Inducible Factor 1 Alpha (HIF1a); Porcine Hypoxia Inducible Factor 1 Alpha (HIF1a) ELISA Kit; HIF1a elisa kit

• Reactivity: Porcine

• Preparation and Storage: Store all reagents at 2-8 degree C

NCBI and Uniprot Product Information

• NCBI GI #: 117935055
• NCBI GeneID: 281814
• NCBI Accession #: NP_776764.2
• NCBI GenBank Nucleotide #: NM_174339.3
• UniProt Accession #: Q9XTA5
• Molecular Weight: 92,128 Da
• NCBI Official Full Name: hypoxia-inducible factor 1-alpha
• NCBI Official Synonym Full Names: hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)<
• NCBI Official Symbol: HIF1A
• NCBI Protein Information: hypoxia-inducible factor 1-alpha; HIF1 alpha; HIF1-alpha; HIF-1 alpha; HIF-1-alpha; hypoxia-inducible factor 1 alpha; hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
• UniProt Protein Name: Hypoxia-inducible factor 1-alpha
• Protein Family: Hypoxia-inducible factor
• UniProt Gene Name: HIF1A
• UniProt Synonym Gene Names: HIF-1-alpha; HIF1-alpha
• UniProt Entry Name: HIF1A_BOVIN

Uniprot Description

Function: Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia

By similarity.

Subunit structure: Interacts with COPS5 subunit of COP9 signalosome complex, leading to the regulation of its stability. Efficient DNA binding requires heterodimerization of an alpha and a beta/ARNT subunit. Interacts with NCOA1, NCOA2, APEX, HSP90 and TSGA10. Interacts with VHL which docks HFA1 to the E3 ubiquitin ligase complex for subsequent destruction. Interaction, via the ODD domain, with the beta domain of VHLL, protects HIF1A from destruction by competing against the destructive targeting initiated by VHL. Interacts with RORA (via the DNA binding domain); the interaction enhances HIF1A transcription under hypoxia through increasing protein stability. Interaction with PSMA7 inhibits the transactivation activity of HIF1A under both normoxic and hypoxia-mimicking conditions

By similarity. Interacts with USP20. Interacts with GNB2L1/RACK1; promotes HIF1A ubiquitination and proteasome-mediated degradation. Interacts with EP300 (via TAZ-type 1 domain); the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts with CREBBP (via TAZ-type 1 domain)

By similarity. Interacts (via N-terminus) with USP19

By similarity.

Subcellular location: Cytoplasm

By similarity. Nucleus

By similarity. Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia

By similarity.

Domain: Contains two independent C-terminal transactivation domains, NTAD and CTAD, which function synergistically. Their transcriptional activity is repressed by an intervening inhibitory domain (ID)

By similarity.

Post-translational modification: In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD1 and EGLN2/PHD2. EGLN3/PHD3 has also been shown to hydroxylate Pro-564. The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation. Deubiquitinated by USP20. Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization

By similarity.In normoxia, is hydroxylated on Asn-800 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation

By similarity.S-nitrosylation of Cys-797 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex

By similarity.Acetylation of Lys-532 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation

By similarity.Requires phosphorylation for DNA-binding. Phosphorylation at Ser-247 by CSNK1D/CK1 represses kinase activity and impairs ARNT binding. Phosphorylation by GSK3-beta and PLK3 promote degradation by the proteasome

By similarity.The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains

By similarity.Sumoylated; with SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Desumoylation by SENP1 leads to increased HIF1A stability and transriptional activity

By similarity.

Sequence similarities: Contains 1 bHLH (basic helix-loop-helix) domain.Contains 1 PAC (PAS-associated C-terminal) domain.Contains 2 PAS (PER-ARNT-SIM) domains.