SAB5200017

Sigma-Aldrich

Monoclonal Anti-HIF-1 α antibody produced in mouse

clone ESEE122, 1 mg/mL, purified immunoglobulin

Sinónimos:
Anti-HIF1 alpha, ESEE122, Anti-HIF1A, Anti-MOP1, Anti-PASD8, Anti-Hypoxia inducible factor 1 alpha, Anti-ARNT interacting protein
NACRES:
NA.41

Quality Level

biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

ESEE122, monoclonal

form

buffered aqueous glycerol solution

species reactivity

human, rat, bovine, mouse

concentration

1 mg/mL

application(s)

immunocytochemistry: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
indirect immunofluorescence: suitable
western blot: suitable

isotype

IgG1

conjugate

unconjugated

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

mouse ... Hif1a(15251)

General description

Hypoxia-inducible factor-1 α (HIF1 α) gene encodes the α subunit of HIF-1. HIF-1α contains oxygen-dependent degradation (ODD) domain that mediates the interaction between HIF-1α and the E3 ubiquitin ligase complex, which in turn facilitates continuous poly ubiquitination of HIF-1α in normoxic cells. The gene encoding it is localized on human chromosome 14q23.2. HIF1 α belongs to the basic helix-loop-helix family of transcription factors.

Specificity

Specific for HIF1-alpha.

Immunogen

Recombinant fragment corresponding to amino acids 329-530

Application

Monoclonal Anti-HIF-1 α antibody produced in mouse has been used in siRNA assay and western blot analysis.

Biochem/physiol Actions

Hypoxia-inducible factor-1(HIF1) plays an essential role in cellular and systemic homeostatic responses to hypoxia. During hypoxia, the two subunits of this factor undergo post-translational modifications which in turn promote transactivation. HIF-1α gene loss is associated with development of nonpapillary renal carcinomas. The encoded protein functions as a key regulator of the vascular endothelial growth factor (VEGF) under hypoxic response in human stromal cells in vitro. HIF-1α protein expression is often seen in invasive breast cancer. Experimental data demonstrates that downregulation of HIF-1α decreases tumorigenicity of MCF-7 (human breast adenocarcinoma cell line) cells and propose a promising combination of both anti-HIF-1 strategy and traditional chemotherapy to improve cancer treatment.

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Solution in PBS, pH 7.4, 50% glycerol, and 0.09% sodium azide

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point F

Not applicable

Flash Point C

Not applicable

Certificado de Análisis

Certificado de origen

Multiple gastrointestinal stromal and other tumors caused by platelet-derived growth factor receptor alpha gene mutations: a case associated with a germline V561D defect.
Pasini B
The Journal of Clinical Endocrinology and Metabolism, 92, 3728-3732 (2007)
Propofol Through Upregulating Caveolin-3 Attenuates Post-Hypoxic Mitochondrial Damage and Cell Death in H9C2 Cardiomyocytes During Hyperglycemia.
Deng F
Cellular Physiology and Biochemistry, 44, 279-292 (2017)
Significance of chromosome arm 14q loss in nonpapillary renal cell carcinomas.
Herbers J
Genes Chromosomes Cancer, 19, 29-35 (1997)
Regulation of hypoxia-inducible factor 1alpha expression and function by the mammalian target of rapamycin.
Hudson CC
Molecular and Cellular Biology, 22, 7004-7014 (2002)
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, 1341-1351 (2006)

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