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Protein markers are an essential component in biological research and drug development. Whether it is for protein electrophoresis or western blot, our pre-stained protein markers help you quickly determine the molecular weight of the target protein or evaluate the transfer efficiency.
Streptavidin is a tetrameric protein providing 4 high-affinity biotin binding sites. We offer a wide array of products pre-conjugated with streptavidin to support your research as well as biotinylated proteins.
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Name:Hypoxia-inducible factor 1 alpha Target Synonym:ARNT Interacting Protein,HIF-1A,HIF1,Hypoxia-Inducible Factor 1, alpha Subunit,MOP1,HIF-1-alpha,BHLHE78,ARNT-interacting protein,Class E basic helix-loop-helix protein 78,PASD8,HIF1-alpha,HIF1A,Hypoxia Inducible Factor 1 Subunit Alpha,Hypoxia Inducible Fa
Number of Launched Drugs:0 Number of Drugs in Clinical Trials:3 Lastest Research Phase:Phase 2 Clinical
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Synonym Name
HIF-1alpha,HIF1a,MOP1,PASD8,bHLHe78
Background
Hypoxia-inducible factor 1, alpha subunit is also known as ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, PAS domain-containing protein 8, Class E basic helix-loop-helix protein 78 and HIF1A, is a cytoplasm and nucleus protein. HIF1A contains one basic helix-loop-helix (bHLH) domain, one PAC (PAS-associated C-terminal) domain and two PAS (PER-ARNT-SIM) domains. It is expressed in most tissues with highest levels in kidney and heart. is a bHLH - PAS transcription factor found in mammalian cells growing at low oxygen concentrations. It plays an essential role in cellular and systemic responses to hypoxia. This is one of the class of hypoxia inducible factors, a family that includes Hif1a, Hif2a, and Hif3a. HIF1A activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF1A plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. HIF1A interacts with the HIF1A beta / ARNT subunit. Heterodimerization of HIF1A is required for DNA binding. HIF1A interacts with COPS5. The interaction increases the transcriptional activity of HIF1A through increased stability.
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