Mouse anti-Human Hypoxia Inducible Factor 1 alpha Monoclonal Antibody | anti-HIF1A antibody

Hypoxia Inducible Factor 1 alpha (HIF1A, MOP1, PASD8, alpha subunit (basic helix-loop-helix transcription factor), Member of PAS Superfamily 1)

Cat. Num. AAA607085

• Gene Names: HIF1A; HIF1; MOP1; PASD8; bHLHe78; HIF-1alpha; HIF1-ALPHA
• Reactivity: Human
• Applications: Western Blot
• Purity: Affinity Purified; Purified by Protein G affinity chromatography.
• Synonyms: Hypoxia Inducible Factor 1 alpha; Monoclonal Antibody; Hypoxia Inducible Factor 1 alpha (HIF1A; MOP1; PASD8; alpha subunit (basic helix-loop-helix transcription factor); Member of PAS Superfamily 1); Anti -Hypoxia Inducible Factor 1 alpha (HIF1A; anti-HIF1A antibody

• Host: Mouse
• Reactivity: Human
• Clonality: Monoclonal
• Isotype: IgG2a
• Clone Number: 4E144
• Specificity: Recognizes human HIF-1a at ~120KD.
• Purity/Purification: Affinity Purified; Purified by Protein G affinity chromatography.
• Form/Format: Supplied as a liquid in PBS pH 7.2, 50% glycerol.

• Applicable Applications for anti-HIF1A antibody: Western Blot (WB)
• Immunogen: Human HIF-1 alpha amino acids 329-530 fused to GST protein
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, 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 MBS607085: |Lane 1: HeLa Cell Lysate |Lane 2: HeLa+CoCl2 Cell Lysate.)

Related Product Information for anti-HIF1A antibody

Hypoxia inducible factor-1 (HIF-1) is a transcriptional complex which regulates systemic, local and intracellular homeostatic responses elicited by hypoxia. HIF-1 is a heterodimer of HIF-1alpha and HIF-1beta. The molecular mass in denatured SDS-PAGE gels for HIF-1alpha is 120kD and for HIF-1beta between 92-94kD (2). HIF-1 beta is constitutively expressed and serves as a dimerization partner for several other transcription factors. However, HIF-1 alpha is unique to HIF-1 and its expression is tightly regulated by cellular oxygen concentration. HIF-1 alpha is continuously degraded under normoxia conditions by the ubiquitin-proteosome system but under hypoxia conditions. HIF-1alpha is stabilized and activated by posttranslational mechanisms. A diverse group of genes such as erythropoietin, vascular endothelial growth factor (VEGF), glucose transporters, glycolytic pathway enzymes, heme-oxygenase and inducible nitric oxide synthetase share a common mode of regulation which requires binding of HIF-1 to a hypoxia-response element followed by transcriptional activation of the target genes. Many of these genes promote cell survival by expediting O2 delivery to oxygen-deprived tissues by promoting the formation of new vasculature by increasing glucose transport and by raising the levels of glycolytic enzymes.

Product Categories/Family for anti-HIF1A antibody

Antibodies; Abs to Transcription Factors

NCBI and Uniprot Product Information

• NCBI GI #: 4504385
• NCBI GeneID: 3091
• NCBI Accession #: NP_001521.1
• NCBI GenBank Nucleotide #: NM_001530.3
• UniProt Accession #: Q16665; Q53XP6; Q96PT9; Q9UPB1
• Molecular Weight: 92,670 Da
• NCBI Official Full Name: hypoxia-inducible factor 1-alpha isoform 1
• NCBI Official Synonym Full Names: hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
• NCBI Official Symbol: HIF1A
• NCBI Official Synonym Symbols: HIF1; MOP1; PASD8; bHLHe78; HIF-1alpha; HIF1-ALPHA
• NCBI Protein Information: hypoxia-inducible factor 1-alpha; HIF-1-alpha; OTTHUMP00000179061; OTTHUMP00000179062; OTTHUMP00000179063; member of PAS protein 1; ARNT interacting protein; ARNT-interacting protein; member of PAS superfamily 1; PAS domain-containing protein 8; basic-helix-loop-helix-PAS protein MOP1; class E basic helix-loop-helix protein 78; hypoxia-inducible factor 1 alpha isoform I.3; 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: BHLHE78; MOP1; PASD8
• UniProt Entry Name: HIF1A_HUMAN

NCBI Description

This gene encodes the alpha subunit of transcription factor hypoxia-inducible factor-1 (HIF-1), which is a heterodimer composed of an alpha and a beta subunit. HIF-1 functions as a master regulator of cellular and systemic homeostatic response to hypoxia by activating transcription of many genes, including those involved in energy metabolism, angiogenesis, apoptosis, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1 thus plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq]

Uniprot Description

HIF1A: 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. Interacts with the HIF1A beta/ARNT subunit; heterodimerization is required for DNA binding. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability. Interacts with EP300 (via TAZ-type 1 domains); the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts with CREBBP (via TAZ-type 1 domains). Interacts with NCOA1, NCOA2, APEX and HSP90. Interacts (hydroxylated within the ODD domain) with VHLL (via beta domain); the interaction, leads to polyubiquitination and subsequent HIF1A proteasomal degradation. During hypoxia, sumoylated HIF1A also binds VHL; the interaction promotes the ubiquitination of HIF1A. Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription. Interacts (Via the ODD domain) with ARD1A; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia. Interacts with RWDD3; the interaction enhances HIF1A sumoylation. Interacts with TSGA10. 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. Interacts with USP20. Interacts with RACK1; promotes HIF1A ubiquitination and proteasome- mediated degradation. Interacts (via N-terminus) with USP19. Under reduced oxygen tension. Induced also by various receptor-mediated factors such as growth factors, cytokines, and circulatory factors such as PDGF, EGF, FGF2, IGF2, TGFB1, HGF, TNF, IL1B, angiotensin-2 and thrombin. However, this induction is less intense than that stimulated by hypoxia. Repressed by HIPK2 and LIMD1. Expressed in most tissues with highest levels in kidney and heart. Overexpressed in the majority of common human cancers and their metastases, due to the presence of intratumoral hypoxia and as a result of mutations in genes encoding oncoproteins and tumor suppressors. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Autophagy; DNA-binding; Transcription factor

Chromosomal Location of Human Ortholog: 14q23.2

Cellular Component: nucleoplasm; transcription factor complex; cytoplasm; nucleolus; nuclear speck; cytosol; nucleus

Molecular Function: RNA polymerase II transcription factor activity, enhancer binding; histone deacetylase binding; Hsp90 protein binding; transcription factor binding; protein kinase binding; histone acetyltransferase binding; signal transducer activity; protein binding; enzyme binding; sequence-specific DNA binding; protein heterodimerization activity; ubiquitin protein ligase binding; transcription factor activity; nuclear hormone receptor binding

Biological Process: lactation; oxygen homeostasis; response to muscle activity; embryonic placenta development; cellular iron ion homeostasis; positive regulation of transcription, DNA-dependent; signal transduction; glucose homeostasis; positive regulation of vascular endothelial growth factor receptor signaling pathway; muscle maintenance; negative regulation of bone mineralization; connective tissue replacement during inflammatory response; elastin metabolic process; axon transport of mitochondrion; regulation of transcription, DNA-dependent; visual learning; angiogenesis; heart looping; regulation of transcription from RNA polymerase II promoter in response to oxidative stress; neural crest cell migration; negative regulation of growth; hemoglobin biosynthetic process; positive regulation of neuroblast proliferation; regulation of transforming growth factor-beta2 production; Notch signaling pathway; negative regulation of TOR signaling pathway; collagen metabolic process; embryonic hemopoiesis; positive regulation of erythrocyte differentiation; positive regulation of nitric-oxide synthase activity; B-1 B cell homeostasis; digestive tract morphogenesis; mRNA transcription from RNA polymerase II promoter; positive regulation of chemokine production; positive regulation of angiogenesis; neural fold elevation formation; regulation of gene expression; positive regulation of hormone biosynthetic process; cartilage development; positive regulation of glycolysis; lactate metabolic process; response to hypoxia; epithelial to mesenchymal transition; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; cerebral cortex development