SRP2097

Sigma-Aldrich

HIF-1 α, C-terminal activation domain (776-826 human

recombinant, expressed in E. coli, ≥85% (SDS-PAGE)

Sinónimos:
HIF1-alpha, HIF-1alpha, bHLHe78, PASD8, MOP1, HIF1
NACRES:
NA.26
En este momento no podemos mostrarle ni los precios ni la disponibilidad

biological source

human

recombinant

expressed in E. coli

assay

≥85% (SDS-PAGE)

form

frozen liquid

mol wt

~6.7 kDa

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

700 μg/mL

color

colorless to clear

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... HIF1A(3091)

General description

The gene encoding it is localized on human chromosome 14q23.2.

Biochem/physiol Actions

During hypoxia, the two subunits of this factor undergo post-translational modifications which in turn promote transactivation.
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-1α 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. 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). HIF-1alpha protein expression often seen in invasive breast cancer. 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.

Physical form

Clear and colorless frozen liquid solution

Preparation Note

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point F

Not applicable

Flash Point C

Not applicable

Certificado de Análisis
Vascular endothelial growth factor (VEGF) regulation by hypoxia inducible factor-1 alpha (HIF1A) starts and peaks during endometrial breakdown, not repair, in a mouse menstrual-like model
Xihua Chen
Human Reproduction, 30(9), 2160-2170 (2015)
Regulation of Hypoxia-Inducible Factor 1a Expression and Function by the Mammalian Target of Rapamycin
Christine C. Hudson
Molecular and Cellular Biology, 22(20), 7004-7014 (2002)
Multiple Gastrointestinal Stromal and Other Tumors Caused by Platelet-Derived Growth Factor Receptor a Gene Mutations: A Case Associated with a Germline V561D Defect
Barbara Pasini
The Journal of Clinical Endocrinology and Metabolism, 92(9) (2007)
Knockdown of hypoxia-inducible factor-1alpha in breast carcinoma MCF-7 cells results in reduced tumor growth and increased sensitivity to methotrexate.
Li J
Biochemical and Biophysical Research Communications, 342(4), 1341-1351 (2006)
Hypoxia-Inducible Factor (HIF)-1 Regulatory Pathway and its Potential for Therapeutic Intervention in Malignancy and Ischemia
Jennifer E. Ziello
The Yale Journal of Biology and Medicine, 80(2), 51-60 (2007)
Artículos
We present an article about how proliferating cells require the biosynthesis of structural components for biomass production and for genomic replication.
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