Recombinant Proteins
Product List
HIF1A Human (85 a.a.)
Hypoxia-Inducible Factor-1 Alpha (85 a.a.) Human Recombinant
HIF1A Human, His
Hypoxia-Inducible Factor-1 Alpha Human Recombinant, His Tag
HIF1AN Human
Hypoxia-Inducible Factor-1 Alpha Inhibitor Human Recombinant
HIF1AN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-349) and having a molecular mass of 40.2kDa.
The HIF1AN is purified by proprietary chromatographic techniques.
HIF1A Human
Hypoxia-Inducible Factor-1 Alpha Human Recombinant
HIF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (530-826) and having a molecular mass of 32.8kDa. The protein migrates as a 32.8kDa band on SDS-PAGE. The HIF1-A is purified by proprietary chromatographic techniques.
Introduction
Hypoxia-Inducible Factor (HIF) is a transcription factor that responds to changes in cellular oxygen levels. It is a heterodimer composed of an oxygen-sensitive alpha subunit (HIF-α) and a constitutively expressed beta subunit (HIF-β). There are three main isoforms of the alpha subunit: HIF-1α, HIF-2α, and HIF-3α, each with distinct but overlapping roles in hypoxia response.
Key Biological Properties: HIF is crucial for cellular adaptation to low oxygen conditions (hypoxia). It regulates the expression of genes involved in angiogenesis, metabolism, erythropoiesis, and cell survival.
Expression Patterns: HIF-1α is ubiquitously expressed in most tissues, while HIF-2α and HIF-3α have more restricted expression patterns. HIF-2α is primarily found in endothelial cells, kidney, liver, and heart, whereas HIF-3α is less well-characterized but is known to be expressed in the lung and other tissues.
Tissue Distribution: HIF-1α is present in almost all tissues, reflecting its role in general hypoxia response. HIF-2α is more tissue-specific, with high expression in organs involved in oxygen sensing and metabolism.
Primary Biological Functions: HIF regulates genes that control various physiological processes, including angiogenesis (formation of new blood vessels), glycolysis (glucose metabolism), and erythropoiesis (production of red blood cells).
Role in Immune Responses: HIF plays a role in modulating immune responses by regulating the activity of immune cells such as macrophages and T cells. It helps in the adaptation of immune cells to hypoxic conditions often found in inflamed or tumor tissues.
Pathogen Recognition: HIF can influence the expression of genes involved in pathogen recognition and the innate immune response, enhancing the ability of the immune system to respond to infections.
Mechanisms with Other Molecules and Cells: HIF interacts with various co-factors and transcriptional regulators to modulate gene expression. It binds to hypoxia-responsive elements (HREs) in the promoter regions of target genes.
Binding Partners: HIF-α subunits dimerize with HIF-β to form the active transcription factor complex. They also interact with other proteins such as p300/CBP, which are co-activators that enhance transcriptional activity.
Downstream Signaling Cascades: HIF activation leads to the transcription of numerous genes involved in angiogenesis (e.g., VEGF), metabolism (e.g., GLUT1), and survival (e.g., BCL2), which collectively help cells adapt to hypoxic conditions.
Expression and Activity Control: HIF-α subunits are regulated by oxygen-dependent hydroxylation, which marks them for degradation under normoxic conditions. In hypoxia, this hydroxylation is inhibited, allowing HIF-α to stabilize and translocate to the nucleus.
Transcriptional Regulation: HIF-α binds to HREs in the DNA, recruiting co-activators and the transcriptional machinery to initiate gene expression.
Post-Translational Modifications: HIF-α undergoes various post-translational modifications, including hydroxylation, acetylation, and phosphorylation, which influence its stability, localization, and activity.
Biomedical Research: HIF is a key target in cancer research due to its role in tumor growth and survival under hypoxic conditions. It is also studied in the context of cardiovascular diseases, stroke, and chronic kidney disease.
Diagnostic Tools: HIF levels and activity can serve as biomarkers for hypoxia-related conditions, aiding in the diagnosis and prognosis of diseases such as cancer and ischemic disorders.
Therapeutic Strategies: Targeting HIF pathways offers potential therapeutic approaches for treating cancer, promoting wound healing, and managing ischemic diseases. Inhibitors of HIF-1α are being explored as anti-cancer agents.
Development: HIF is essential for embryonic development, particularly in the formation of the cardiovascular system and the placenta, which are highly dependent on oxygen supply.
Aging: HIF activity declines with age, which may contribute to age-related diseases and reduced regenerative capacity.
Disease: Dysregulation of HIF is implicated in various diseases, including cancer, where it promotes tumor growth and metastasis, and chronic diseases like pulmonary hypertension and heart failure.
