Anti-HIF1a
568 EUR
In Stock
quantity
Produktdetaljer
Katalognummer: 894 - AB0070-100
Produktkategori: Företag och industri > Vetenskap och laboratorium
Gentaur
Storlek: 300 µg
Parameters
| Additional information | Purification: Epitope affinity purified;Immunogen: Purified recombinant peptide derived from within residues 470 to 590 aa of human HIF1a produced in E. coli.;Specificity test:Detects HIF1a in transfected cells and a band of approximately 120 kDa by Western blot in cell lysates.;Buffer: PBS, 20% glycerol and 0.05% sodium azide;References: 1. Ramalho AR, Toscano A, Pereira P. et al. Rev Port Cardiol. 2017 May. PMID:28479269 |
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| Storage and shipping | Store at -20 C for long-term storage. Store at 2-8 C for up to one month. |
AB0070-100
Anti-HIF1a
Goat polyclonal to 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 apoptosis, angiogenesis, energy metabolism, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1 thus plays an essential role in tumour angiogenesis, embryonic vascularization, and pathophysiology of ischemic disease.
568 €
AB0112-200
Anti-HIF1a
Goat polyclonal to 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 apoptosis, angiogenesis, energy metabolism, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1 thus plays an essential role in tumour angiogenesis, embryonic vascularization, and pathophysiology of ischemic disease.
568 €
ET7108-50
Anti-HIF1AN Antibody [JG37-66]
Factor inhibiting HIF-1 (FIH-1) exists as a homodimer and binds to HIF-1α. Specifically, FIH-1 operates as an asparaginyl hydroxylase. It catalyzes the hydroxylation of the β-carbon of Asparagine residue 803 within the carboxy terminal transactivation domain of HIF-1α. This hydroxylation event blocks the association of HIF-1α with co-activators. FIH-1 also binds to von Hippel-Lindau (VHL) tumor suppressor protein, which represses transcriptional ac-tivity of HIF-1α. In transiently transfected human osteosarcoma cells, FIH-1 localizes to the cytoplasm. The structure of FIH-1 includes a jellyroll-like β-barrel containing ferrous-binding triad residues. The gene encoding human FIH-1 maps to chromosome 10q24.
496.5 €
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