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Hypoxia Inducible Factor 1, alpha Subunit (Basic Helix-Loop-Helix Transcription Factor) (HIF1A) (Internal Region) antibody

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Antigen
  • hif1a
  • AA959795
  • HIF1alpha
  • MOP1
  • bHLHe78
  • HIF-1A
  • HIF-1alpha
  • HIF1
  • HIF1-ALPHA
  • PASD8
  • HIF1-alpha
  • hif-1a
  • hypoxia inducible factor 1 alpha
  • hypoxia inducible factor 1, alpha subunit
  • hypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
  • hypoxia-inducible factor 1 alpha
  • hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
  • Protein HIF-1
  • hif-1a
  • Hif1a
  • HIF1A
  • hif-1
Alternatives
anti-Human Hypoxia Inducible Factor 1, alpha Subunit (Basic Helix-Loop-Helix Transcription Factor) antibody for Electrophoretic Mobility-Shift Assay
Epitope
Internal Region
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59
40
32
20
18
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13
10
8
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3
2
2
2
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2
2
2
1
1
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Reactivity
Human
610
297
250
145
92
77
66
64
58
54
43
37
29
21
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18
16
16
7
3
2
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1
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Host
Rabbit
383
279
2
Clonality
Polyclonal
Conjugate
Un-conjugated
51
33
33
26
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25
17
17
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14
12
12
6
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6
4
4
4
4
2
2
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2
2
2
2
2
2
2
2
2
2
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2
1
1
1
1
1
1
1
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1
Application
Immunohistochemistry (IHC), Western Blotting (WB)
518
229
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184
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170
107
91
62
16
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13
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13
10
7
6
5
4
3
3
2
2
2
1
1
Options
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Immunogen A synthetic peptide from the internal region of human HIF1 alpha conjugated to an immunogenic carrier protein was used as the antigen. The antigen shares 94% identity with rat and mouse sequences.
Specificity Specific for HIF1A.
Purification Whole serum
Alternative Name HIF1 alpha (HIF1A Antibody Abstract)
Background Function: Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions activates the transcription of over 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBPB and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP.
Subcellular location: Cytoplasm. Nucleus. Note: Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia.
Tissue specificity: Expressed in most tissues with highest levels in kidney and heart. Overexpressed in the majority of common human cancers and their metastases, due to the presence of intratumoral hypoxia and as a result of mutations in genes encoding oncoproteins and tumor suppressors. Also known as: Hypoxia-inducible factor 1 alpha, HIF-1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1.
Research Area Cancer, Transcription Factors
Pathways Positive Regulation of Peptide Hormone Secretion, Regulation of Hormone Metabolic Process, Regulation of Hormone Biosynthetic Process, Cellular Response to Molecule of Bacterial Origin, Carbohydrate Homeostasis, Transition Metal Ion Homeostasis
Application Notes A dilution of 1 : 300 to 1 : 2000 is recommended.
The optimal dilution should be determined by the end user.
Not yet tested in other applications.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Background publications Hon, Wilson, Harlos, Claridge, Schofield, Pugh, Maxwell, Ratcliffe, Stuart, Jones: "Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL." in: Nature, Vol. 417, Issue 6892, pp. 975-8, 2002 (PubMed).

Huang, Gu, Schau, Bunn: "Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, Issue 14, pp. 7987-92, 1998 (PubMed).

Hogenesch, Chan, Jackiw, Brown, Gu, Pray-Grant, Perdew, Bradfield: "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway." in: The Journal of biological chemistry, Vol. 272, Issue 13, pp. 8581-93, 1997 (PubMed).

Jiang, Zheng, Leung, Roe, Semenza: "Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension." in: The Journal of biological chemistry, Vol. 272, Issue 31, pp. 19253-60, 1997 (PubMed).

Wang, Jiang, Rue, Semenza: "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).