HIF-1a NTAD (530-698)

• Species: Human
• Expression Host: E.coli
• Tag: His-tag
• Purity: 90%
• Molecular Weight: 19.8 kDa.
• Gene Accession Number: NM_001530.

Purification and Quality Control
The purified recombinant protein is greater than 95% homogeneous based on SDS-PAGE analysis.
The His tagged HIF-1α-CTAD was expressed in an E. coli system and purified by affinity and FPLC chromatography.

Unit Definition (Activity)
1 unit equals 1 nano-gram of purified protein. variable in different lots

Applications
Recombinant HIF-1α can be used for protein-protein interaction assays; for in vitro transcription assays and for cell growth assays.

Formulation and Storage
1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA

Synonym
bHLHe78; HIF-1alpha; HIF1 and HIF1-ALPHA.

Protein Sequence
SDLACRLLGQ SMDESGLPQL TSYDCEVNAP IQGSRNLLQG EELLRALDQV N

Background
Hypoxia-inducible factor-1 (HIF1) is a transcription factor found in mammalian cells cultured under reduced oxygen tension that plays an essential role in cellular and systemic homeostatic responses to hypoxia. HIF1 is a heterodimer composed of an alpha subunit and a beta subunit. The beta subunit has been identified as the aryl hydrocarbon receptor nuclear translocator (ARNT). This gene encodes the alpha subunit of HIF-1. HIF-1 alpha contains two transactivation domains located between amino acids 531 and 826. Overexpression of a natural antisense transcript (aHIF) of this gene has been shown to be associated with nonpapillary renal carcinomas. Two alternative transcripts encoding different isoforms have been identified. Specific disruption of the HIF-1 pathway is important for exploring its role in tumor biology and developing more efficient weapons to treat cancer (1). HIF-1alpha is a master regulator of the hypoxic response, and its proangiogenic activities include, but are not limited to, regulation of vascular endothelial growth factor (VEGF) (2). HIF-1alpha protein expression often seen in invasive breast cancer (3). Recent data demonstrates that HIF-1alpha knockdown reduces tumorigenicity of MCF-7 cells and suggest a promising combination of both anti-HIF-1 strategy and traditional chemotherapy to improve cancer treatment (4).

References:
1. Semenza,G.L. et al., (1994) J. Biol. Chem. 269 (38), 23757-23763
2. Corley,K.M. et al., (2005) J. Cell. Biochem. 96 (5), 971-985
3. Vleugel,M.M., et al., (2005) Cancer Genet. Cytogenet. 163 (2), 168-172
4. Li,J., et al. (2006) Biochem. Biophys. Res. Commun. 342 (4), 1341-1351

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DISCLAIMER

This products is recommended For RESEARCH USE ONLY and is Not qualified for Use in Diagnostic or Therapeutic Procedures.