Hypoxia Inducible Factor 1, alpha Subunit (Basic Helix-Loop-Helix Transcription Factor) (HIF1A) (AA 610-727) antibody
|Synonyms||HIF1, MOP1, PASD8, bHLHe78, HIF-1alpha, HIF1-ALPHA, HIF1A, HIF-1a, HIF1a, hif-1a, hif1a|
Alternatives Western Blotting (WB), Immunofluorescence (IF)
|6 references available|
|Quantity||50 µg (250 µg/ml) (Variants)|
|Price||Product not available in this region.|
Molecular oxygen (O2) is essential for mammalian metabolic processes such as oxidative phosphorylation. Thus, survival depends upon instantaneous transcriptional modulation of genes that maintain O2 homeostasis. Transcriptional control of several of these genes is mediated by hypoxia-inducible factor 1 (HIF-1). HIF-1 is a heterodimer whose alpha and beta subunits are members of the PAS family of basic helix-loop-helix (bHLH) transcription factors. Common structural features of these proteins are an N-terminal bHLH DNA-binding domain and multiple PAS domains that confer dimerization ability and target gene specificity. Members diverge in their C-terminal regions. HIF-1beta is also known as the arylhydrocarbon nuclear translocator which is part of the functional dioxin receptor. However, HIF-1alpha functions exclusively to mediate responses to O2 deprivation. It contains C-terminal and internal transactivation domains. Although HIF-1 aproteinlevels increase during hypoxia, it is unstable in the presence of O2 due to an oxygen-dependent degradation domain (ODD) that targets it for ubiquitination. Thus, HIF-1alpha is essential for functional HIF-1 to mediate gene transcription in response to hypoxia.
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
|Molecular Weight||120 kDa|
Related Products: ABIN967389
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution containing BSA, glycerol.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at -20° C.|
|Restrictions||For Research Use only|
|Western blot analysis of HIF-1alpha on HeLa cells stimulated with CoCl2 lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of HIF-1alpha.|
Wang, Jiang, Rue et al.: "Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, Issue 12, pp. 5510-4, 1995 (PubMed).
Srinivas, Leshchinsky, Sang et al.: "Oxygen sensing and HIF-1 activation does not require an active mitochondrial respiratory chain electron-transfer pathway." in: The Journal of biological chemistry, Vol. 276, Issue 25, pp. 21995-8, 2001 (PubMed).
Wiesener, Münchenhagen, Berger et al.: "Constitutive activation of hypoxia-inducible genes related to overexpression of hypoxia-inducible factor-1alpha in clear cell renal carcinomas." in: Cancer research, Vol. 61, Issue 13, pp. 5215-22, 2001 (PubMed).
Arsham, Plas, Thompson et al.: "Phosphatidylinositol 3-kinase/Akt signaling is neither required for hypoxic stabilization of HIF-1 alpha nor sufficient for HIF-1-dependent target gene transcription." in: The Journal of biological chemistry, Vol. 277, Issue 17, pp. 15162-70, 2002 (PubMed).
Sánchez-Elsner, Botella, Velasco et al.: "Endoglin expression is regulated by transcriptional cooperation between the hypoxia and transforming growth factor-beta pathways." in: The Journal of biological chemistry, Vol. 277, Issue 46, pp. 43799-808, 2002 (PubMed).
Eckard, Dai, Wu et al.: "Effects of cellular iron deficiency on the formation of vascular endothelial growth factor and angiogenesis. Iron deficiency and angiogenesis." in: Cancer cell international, Vol. 10, pp. 28, 2010 (PubMed).