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

Antigen: Hypoxia Inducible Factor 1, alpha Subunit (Basic Helix-Loop-Helix Transcription Factor) (HIF1A)

Synonyms: HIF1, MOP1, PASD8, bHLHe78, HIF-1alpha, HIF1-ALPHA, HIF1A, HIF-1a, HIF1a, hif-1a, hif1a

Epitope: internal

Clonality: Polyclonal

Host: Rabbit

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN350369

Additional Information

Alternative name: HIF1alpha (HIF1A, MOP1, Hypoxia-inducible factor 1alpha) (internal region)

Swiss-Prot: Q16665

Immunogen: A synthetic peptide from the internal region of human HIF1 alpha (HIF1A, MOP1, Hypoxia-inducible factor 1 alpha) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen shares 94% identity with rat and mouse sequences.

Format: Lyophilized

Description: 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.

Specificity: Appears to be specific for HIF1A.

Application Details

Application Notes: IHC, WB. 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.

Purity: whole serum

Storage: 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.

Restrictions: For Research Use only

Publications

Publications: 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).

Hogenesch, Chan, Jackiw et al.: "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 et al.: "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).

Huang, Gu, Schau et al.: "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).

Hon, Wilson, Harlos et al.: "Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL." in: Nature, Vol. 417, Issue 6892, pp. 975-8, 2002 (PubMed).