antibody

Hypoxia Inducible Factor 1a (HIF-1a) (BSA & Azide Free)

MBS603203

0.1 mg

710 USD

monoclonal

mouse

nonconjugated

[0.N.329]

human, mouse, rat

Antibody

Hypoxia Inducible Factor 1a (HIF-1a) (BSA & Azide Free)

[Hypoxia Inducible Factor 1a]

[Anti -Hypoxia Inducible Factor 1a (HIF-1a) (BSA & Azide Free)]

[Hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor); Hypoxia-inducible factor 1-alpha; 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); hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor); ARNT-interacting protein; Basic-helix-loop-helix-PAS protein MOP1; Class E basic helix-loop-helix protein 78; bHLHe78; Member of PAS protein 1; PAS domain-containing protein 8]

[HIF1A; HIF1A; HIF1; MOP1; PASD8; bHLHe78; HIF-1alpha; HIF1-ALPHA; BHLHE78; MOP1; PASD8]

HIF1A_HUMAN

Monoclonal

IgG2b,k

[0.N.329]

Mouse

Ferret, Mouse, Rat, Sheep

Recognizes the alpha subunit of HIF-1

Highly Purified. Purified by Protein A affinity chromatography.

Supplied as a liquid in PBS, pH 7.4. No preservatives added. No stabilizing proteins added. Also available with BSA and azide.

1mg/ml

May be stored at 4 degree C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20 degree C or colder. 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.

Suitable for use in Immunohistochemistry. Dilution: Immunohistochemistry: paraffin

Type: Mab. Immunogen: Recombinant protein corresponding to residues 432-528 of hHIF-1a. Cellular Localization: Nuclear

Positive Control: Placenta, melanoma, hemangioma and angiosarcoma. Cellular Localization: Nuclear/Cytoplasmic

Antibodies; Abs to Transcription Factors

Hypoxia-inducible factor-1 (HIF-1). HIF-1 is a heterodimer consisting of an alpha and a beta subunit, both belonging to the basic-helix-loop-helix Per-aryl hydrocarbon receptor nuclear translocator-Sim (PAS) family of transcription factors. HIF-1 is a key component of a widely operative transcriptional response activated by hypoxia, cobaltous ions, and iron chelation. HIF-1 activates transcription of hypoxia-inducible genes, including those encoding: erythropoietin, vascular endothelial growth (VEGF), heme oxygenase-1, inducible nitric oxide synthase, and the glycolytic enzymes aldolase A, enolase 1, lactate dehydrogenase A, phosphofructokinase I, and phosphoglycerate kinase 1. The C-terminal of HIF-1 alpha binds to p300. p300/CBP-HIF complexes participate in the induction of hypoxia-responsive genes, including VEGF.

15214788

Q16665

92,670 Da

Adipogenesis Pathway (198832); Angiogenesis Pathway (198772); HIF-1-alpha Transcription Factor Network Pathway (138045); Hypoxic And Oxygen Homeostasis Regulation Of HIF-1-alpha Pathway (138056); Notch-mediated HES/HEY Network Pathway (169347); PDGFR-beta Signaling Pathway (138071); Pathways In Cancer (83105); Renal Cell Carcinoma Pathway (83107); Renal Cell Carcinoma Pathway (519); Signaling Events Mediated By VEGFR1 And VEGFR2 Pathway (137940)

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]

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: Transcription factor; Autophagy; DNA-binding. Chromosomal Location of Human Ortholog: 14q23.2. Cellular Component: nucleoplasm; transcription factor complex; cytoplasm; nucleolus; nuclear speck; nucleus; cytosol. Molecular Function: RNA polymerase II transcription factor activity, enhancer binding; histone deacetylase binding; Hsp90 protein binding; protein kinase binding; transcription factor binding; histone acetyltransferase binding; protein binding; signal transducer activity; enzyme binding; protein heterodimerization activity; sequence-specific DNA binding; 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; elastin metabolic process; connective tissue replacement during inflammatory response; axon transport of mitochondrion; regulation of transcription, DNA-dependent; visual learning; heart looping; angiogenesis; 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; Notch signaling pathway; regulation of transforming growth factor-beta2 production; 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; cartilage development; positive regulation of hormone biosynthetic process; lactate metabolic process; positive regulation of glycolysis; 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

0.1 mg

710 USD