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Purified Mouse Anti-Human HIF-1α
Purified Mouse Anti-Human HIF-1α
Western blot analysis of HIF-1α on lysate from HeLa stimulated with CoCl2, cobalt chloride. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the Mouse Anti- Human HIF-1α antibody.
Western blot analysis of HIF-1α on lysate from HeLa stimulated with CoCl2, cobalt chloride. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the Mouse Anti- Human HIF-1α antibody.
製品詳細
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BD Transduction Laboratories™
HIF1; HIF-1A; HIF1A; HIF-1-alpha; HIF1-alpha; BHLHE78; MOP1; PASD8
Human (QC Testing)
Mouse IgG1, κ
Human HIF-1α aa. 610-727
Western blot (Routinely Tested), Immunofluorescence (Tested During Development)
120 kDa
250 µg/ml
AB_398272
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
  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. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
610959 Rev. 3
抗体の詳細
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54/HIF-1α

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 α and β 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-1β is also known as the arylhydrocarbon nuclear translocator which is part of the functional dioxin receptor. However, HIF-1α 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-1α is essential for functional HIF-1 to mediate gene transcription in response to hypoxia.

610959 Rev. 3
フォーマットの詳細
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
610959 Rev.3
引用&参考文献
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Development References (7)

  1. Arsham AM, Plas DR, Thompson CB, Simon MC. Phosphatidylinositol 3-kinase/Akt signaling is neither required for hypoxic stabilization of HIF-1 alpha nor sufficient for HIF-1-dependent target gene transcription. J Biol Chem. 2002; 277(17):15162-15170. (Biology: Western blot). View Reference
  2. Effects of cellular iron deficiency on the formation of vascular endothelial growth factor and angiogenesis. Iron deficiency and angiogenesis. Cancer Cell. 10(28)(Biology: Western blot). View Reference
  3. Fallone F, Britton S, Nieto L, Salles B, Muller C. ATR controls cellular adaptation to hypoxia through positive regulation of hypoxia-inducible factor 1 (HIF-1) expression. Oncogene. 2013; 32(37):4387-4396. (Clone-specific: Western blot). View Reference
  4. Sanchez-Elsner T, Botella LM, Velasco B, Langa C, Bernabeu C. Endoglin expression is regulated by transcriptional cooperation between the hypoxia and transforming growth factor-beta pathways. J Biol Chem. 2002; 277(46):43799-43808. (Biology: Immunoprecipitation, Western blot). View Reference
  5. Srinivas V, Leshchinsky I, Sang N, King MP, Minchenko A, Caro J. Oxygen sensing and HIF-1 activation does not require an active mitochondrial respiratory chain electron-transfer pathway. J Biol Chem. 2002; 276(25):21995-21998. (Biology: Immunofluorescence, Western blot). View Reference
  6. Wang GL, Jiang BH, Rue EA, Semenza GL. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci U S A. 1995; 92(12):5510-5514. (Biology). View Reference
  7. Wiesener MS, Munchenhagen PM, Berger I, et al. Constitutive activation of hypoxia-inducible genes related to overexpression of hypoxia-inducible factor-1alpha in clear cell renal carcinomas. Cancer Res. 2001; 61(13):5215-5222. (Biology: Immunohistochemistry, Western blot). View Reference
すべて表示する (7) 表示項目を減らす
610959 Rev. 3

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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.