Anti-HIF-1-alpha/HIF1A Antibody Picoband®

HIF-1α (Hypoxia-inducible factor 1α, HIF1A) is a transcription factor that mediates cellular and systemic homeostatic responses to reduced O2 availability in mammals, including angiogenesis, erythropoiesis and glycolysis. This gene was mapped to 14q21-q24. HIF-1α transactivate genes required for energy metabolism and tissue perfusion and is necessary for embryonic development and tumor explant growth. HIF-1alpha is over expressed during carcinogenesis, myocardial infarction and wound healing. It is crucial for the cellular response to hypoxia and is frequently over expressed in human cancers, resulting in the activation of genes essential for cell survival. HIF-1α regulates the survival and function in the inflammatory microenvironment ly. It is a transcription factor that plays a pivotal role in cellular adaptation to changes in oxygen availability.

Hypoxia-inducible factor 1-alpha; HIF-1-alpha; HIF1-alpha; 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; BHLHE78, MOP1, PASD8

A synthetic peptide corresponding to a sequence at the C-terminal of human HIF-1-alpha, different from the related mouse and rat sequences by three amino acids.

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. A higher level expression seen in pituitary tumors as compared to the pituitary gland. .

Apoptosis, Cancer, Cancer Metabolism, Cardiovascular, Cell Biology, Cell Death, Domain Families, Epigenetics and Nuclear Signaling, Hlh/Leucine Zipper, Host-Virus Interaction, Hypoxia, Interspecies Interaction, Intracellular, Invasion/Microenvironment, Metabolism, Metabolism Processes, Microbiology, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Pathways and Processes, Response To Hypoxia, Transcription

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. .

1. Sutter, C. H.; Laughner, E.; Semenza, G. L. : Hypoxia-inducible factor 1-alpha protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations. Proc. Nat. Acad. Sci. 97: 4748-4753, 2000. 2. Elson, D. A.; Thurston, G.; Huang, L. E.; Ginzinger, D. G.; McDonald, D. M.; Johnson, R. S.; Arbeit, J. M. : Induction of hypervascularity without leakage or inflammation in transgenic mice overexpressing hypoxia-inducible factor-1-alpha. Genes Dev. 15: 2520-2532, 2001. 3. Koshiji, M.; To, K. K.-W.; Hammer, S.; Kumamoto, K.; Harris, A. L.; Modrich, P.; Huang, L. E. : HIF-1-alpha induces genetic instability by transcriptionally downregulating MutS-alpha expression. Molec. Cell 17: 793-803, 2005. 4. Ivan, M.; Kondo, K.; Yang, H.; Kim, W.; Valiando, J.; Ohh, M.; Salic, A.; Asara, J. M.; Lane, W. S.; Kaelin, W. G., Jr. : HIF-alpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O (2) sensing. Science 292: 464-468, 2001.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.

Cytoplasm. Nucleus. Nucleus speckle . Colocalizes with HIF3A in the nucleus and speckles (By similarity) . Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia. .