Product Overview
HIF1A Antibody
Antibodies that detect HIF1A can be used in several scientific applications, including Western Blot, Immunocytochemistry, Immunohistochemistry (Paraffin), Immunohistochemistry (Frozen) and Immunoprecipitation.
These antibodies target HIF1A in Human, Mouse, Rat, Bovine and Non-human primate samples. Our HIF1A monoclonal, polyclonal, recombinant monoclonal and recombinant polyclonal antibodies are developed in Mouse, Rabbit and Goat.
These antibodies have been verified by Cell treatment, Knockdown, Knockout and Relative expression to confirm specificity to HIF1A. Find the HIF1A antibody that fits your needs. Choose from 1 of 54 HIF1A antibodies, which have been validated in experiments with 394 publications and 172 images featured in our data gallery.
Browse primary antibodies for WB, Flow, IHC, ICC/IF, ELISA, IP, and other applications. Antibodies with Advanced Verification data have been validated for specificity to ensure that the antibody binds to the antigen stated. If you cannot find the antibody you're looking for, contact us today to develop custom antibodies for specific targets, species and applications.
Target Information
HIF1-alpha (HIF1A) is a subunit of HIF1, which is a transcription factor found in mammalian cells cultured under reduced oxygen tension. HIF-1 is a heterodimer consisting of an alpha and beta subunit, both belonging to the basic-helix-loop-helix Per-aryl hydrocarbon receptor nuclear translocator-Sim (PAS) family of transcription factors. HIF1 functions as a transcriptional regulator of the adaptive response to hypoxia.
Under hypoxic conditions, HIF-1 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. HIF1-alpha regulates hypoxia-mediated apoptosis, cell proliferation and tumor angiogenesis.
Hypoxia which induces p53 protein accumulation, directly interacts with HIF1-alpha and reduces hypoxia-induced expression of HIF1-alpha by promoting MDM2-mediated ubiquitination and proteasomal degradation under hypoxic conditions. Recent studies suggest that induction of NOX4 by HIF1-alpha contributes to maintain ROS levels after hypoxia and hypoxia-induced proliferation. In humans, it is located on the q arm of chromosome 14.
The C-terminal of HIF1A binds to p300. p300/CBP-HIF complexes participate in the induction of hypoxia-responsive genes, including VEGF. Hypoxia contributes significantly to the pathophysiology of major categories of human disease, including myocardial and cerebral ischemia, cancer, pulmonary hypertension, congenital heart disease and chronic obstructive pulmonary disease.
