HIF1A Human, His
Description
Product Specs
Product Science Overview
HIF-1α is a basic helix-loop-helix PAS domain-containing protein. It is considered the master transcriptional regulator of cellular and developmental responses to hypoxia . The protein structure includes a nuclear localization signal motif, two transactivating domains (CTAD and NTAD), and an intervening inhibitory domain (ID) that can repress the transcriptional activities of CTAD and NTAD .
Under normal oxygen conditions, HIF-1α is rapidly degraded. However, in hypoxic conditions, it stabilizes and translocates to the nucleus, where it dimerizes with HIF-1β. This complex then binds to hypoxia-responsive elements (HREs) in the promoter regions of target genes, activating the transcription of genes involved in various adaptive responses, including angiogenesis, erythropoiesis, and glycolysis .
The dysregulation and overexpression of HIF-1α have been heavily implicated in cancer biology and other pathophysiologies. It plays a critical role in areas such as vascularization and angiogenesis, energy metabolism, cell survival, and tumor invasion . Additionally, HIF-1α is essential for normal placental development in early gestation .
The recombinant form of HIF-1α, tagged with a His (histidine) tag, is used in various research applications. The His tag facilitates the purification of the protein using affinity chromatography, making it easier to study its structure and function in detail. This recombinant protein is crucial for investigating the regulatory mechanisms of HIF-1α and its role in hypoxia-related diseases .
Research on HIF-1α has significant therapeutic potential, particularly in cancer treatment. By understanding how HIF-1α regulates the cellular response to hypoxia, scientists can develop targeted therapies to inhibit its activity in tumors, potentially limiting cancer progression and metastasis .
In conclusion, Hypoxia-Inducible Factor-1 Alpha (Human Recombinant, His Tag) is a vital tool in hypoxia research, providing insights into the molecular mechanisms of oxygen homeostasis and its implications in various diseases.
