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|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Hypoxia Inducible Factor 1, alpha Subunit (Basic Helix-Loop-Helix Transcription Factor) (HIF1A) antibody
|Synonyms||HIF1, MOP1, PASD8, bHLHe78, HIF-1alpha, HIF1-ALPHA, HIF1A, HIF-1a, HIF1a, hif-1a, hif1a|
|Clonality||Monoclonal (4 clones)|
Alternatives Western Blotting (WB)
|12 references available|
|Quantity||5 vials andere|
|Price||Product not available in this region.|
|Alternative name||HIF1A / HIF1 alpha sampler|
NB100-105, NB100-134 = Fusion protein containing amino acids 432-528 of humanHIF-1 alpha.
NB100-296 = Fusion protein containing amino acids 329-530 of human HIF-1alpha.
NB100-449 = A synthetic peptide mapping to a region between residues 775 and theC-terminus (residue 826) of human hypoxia-inducible factor 1, alpha subunit using thenumbering given in Swiss-Prot entry Q16665 (GeneID 3091).
ABIN151926 = A fusion protein including residues 530-825 of the mouse HIF-1 alphaprotein.
|Description||Hypoxia contributes significantly to the pathophysiology of major categories of humandisease, including myocardial and cerebral ischemia, cancer, pulmonary hypertension,congenital heart disease and chronic obstructive pulmonary disease.HIF-1 is a nuclear protein that activates gene transcription in response to reducedcellular 02 concentration. HIF-1 activates the transcription of EPO, VEGF, iNOS, hemeoxygenase 1 and several other critical intracellular responses to hypoxia. HIF-1 is aheterodimer composed of HIF-1a and HIF-1b subunits. Both subunits are induced byhypoxia and rapidly decay upon return to normoxia and are basic-helix-loop-helix-PASproteins. Recent research indicates the ability to regulate hypoxia-inducible factors maybe related to tumor-related angiogenesis in certain cancers.|
|Specificity||These antibodies are specific for HIF-1 alpha. Species Reactivity: NB 100-105 recognizes human, sheep, mouse, rat, rabbit, ferret and bovine.NB 100-479 recognizes human, mouse, monkey and rat.NB 100-134 recognizes human and rat.NB 100-296 recognizes human.ABIN151900 recognizes human and mouse.|
|Application Notes||By Western blot, these antibodies recognize a band ~120 kDa, representing HIF-1 alphain induced tissues and cells. Multiple bands may be seen at 120 kDa representingpost-translational modification of HIF-1 alpha. Suggested working dilutions: *Western Blot - 1:500 -1:1,000 ****Nuclear extracts should be used for Western analysis.|
|Buffer||0.025 ml samples of each antibody|
|Storage||Store at 4C. Do not freeze.|
|Restrictions||For Research Use only|
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Joegi, uora, Nilsson et al.: "Hypoxia alters gene expression in human neuroblastoma cells toward an immature and neural crest-like phenotype." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 10, pp. 7021-6, 2002 (PubMed).
Kong, Eltzschig, Karhausen et al.: "Leukocyte adhesion during hypoxia is mediated by HIF-1-dependent induction of beta2 integrin gene expression." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 28, pp. 10440-5, 2004 (PubMed).
Covello, Simon, Keith: "Targeted replacement of hypoxia-inducible factor-1alpha by a hypoxia-inducible factor-2alpha knock-in allele promotes tumor growth." in: Cancer research, Vol. 65, Issue 6, pp. 2277-86, 2005 (PubMed).
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Galabova-Kovacs, Matzen, Piazzolla et al.: "Essential role of B-Raf in ERK activation during extraembryonic development." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, Issue 5, pp. 1325-30, 2006 (PubMed).
Chade, Zhu, Mushin et al.: "Simvastatin promotes angiogenesis and prevents microvascular remodeling in chronic renal ischemia." in: The FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 20, Issue 10, pp. 1706-8, 2006 (PubMed).
Villanueva, Cespedes, Gonzalez et al.: "bFGF induces an earlier expression of nephrogenic proteins after ischemic acute renal failure." in: American journal of physiology. Regulatory, integrative and comparative physiology, Vol. 291, Issue 6, pp. R1677-87, 2006 (PubMed).
Grimmer, Balbus, Lang et al.: "Regulation of type II collagen synthesis during osteoarthritis by prolyl-4-hydroxylases: possible influence of low oxygen levels." in: The American journal of pathology, Vol. 169, Issue 2, pp. 491-502, 2006 (PubMed).
Wang, Kiss, Franklin et al.: "Different cellular traffic of LDL-cholesterol and acetylated LDL-cholesterol leads to distinct reverse cholesterol transport pathways." in: Journal of lipid research, Vol. 48, Issue 3, pp. 633-45, 2007 (PubMed).