WebGet better batch-to-batch reproducibility with a recombinant antibody. Anti-HIF-1 alpha antibody [EPR16897] (ab179483) Research with confidence – consistent and reproducible results with every batch. Long-term and scalable supply – powered by recombinant technology for fast production. Success from the first experiment – confirmed ... Web14 de mar. de 2012 · Acute tubular necrosis (ATN) caused by ischemia/reperfusion (I/R) during renal transplantation delays allograft function. Identification of factors that mediate protection and/or epithelium recovery could help to improve graft outcome. We studied the expression, regulation and role of hypoxia inducible factor 1-alpha (HIF-1 α), using in …
Hif-1α Knockdown Reduces Glycolytic Metabolism and Induces
Web16 de jun. de 2003 · Hydroxylates HIF-1 alpha at 'Asn-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Web25 de mar. de 2024 · Ryan, H. E., Lo, J. & Johnson, R. S. HIF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J 17 , 3005–3015 (1998). Article CAS PubMed PubMed Central Google Scholar magazine picsou prix
HIF-1 alpha
Web6 de out. de 2024 · HIF is a transcription factor that plays an essential role in the cellular response to low oxygen, orchestrating a metabolic switch that allows cells to survive in this environment. In immunity, infected and inflamed tissues are often hypoxic, and HIF helps immune cells adapt. HIF-α stabilization ca … The Role of HIF in Immunity and Inflammation Web3 de abr. de 2024 · This gene encodes the alpha subunit of transcription factor hypoxia-inducible factor-1 (HIF-1), which is a heterodimer composed of an alpha and a beta subunit. HIF-1 functions as a master regulator of cellular and systemic homeostatic response to hypoxia by activating transcription of many genes, including those involved in energy ... WebWe show that ABL kinases phosphorylate and interact with CUL4A, a cullin ring ligase adaptor, and compete with CPSF1 for CUL4A binding, leading to increased HIF-1α protein levels. Further, we identified the MYC proto-oncogene protein as a second CPSF1 substrate and show that active ABL kinase protects MYC from CPSF1-mediated degradation. magazine piese auto cluj napoca