Render Target: STATIC
Render Timestamp: 2024-12-20T12:23:32.619Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-10-16 17:30:20.990
Product last modified at: 2024-12-17T19:03:07.372Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

HIF-2α (E7K6E) Rabbit mAb #87179

Filter:
  • WB
  • ChIP

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 120
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • ChIP-Chromatin Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    For optimal ChIP and ChIP-Seq results, use 5 μL of antibody and 10 μg of chromatin (approximately 4 × 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.
    Application Dilution
    Western Blotting 1:1000
    Chromatin IP 1:100
    Chromatin IP-seq 1:100

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    HIF-2α (E7K6E) Rabbit mAb recognizes endogenous levels of total HIF-2α protein. This antibody does not cross-react with HIF-1α protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu645 of human HIF-2α protein.

    Background

    Hypoxia-inducible factor (HIF) is essential for the cellular response to hypoxia (1,2). Under normoxia conditions, the α subunit of HIF is ubiquitinated by von Hippel-Lindau (VHL) protein and is degraded in the ubiquitin/proteasome pathway (1,2). Hypoxia inhibits degradation of the α subunit, which leads to its stabilization (1,2). HIF, in turn, regulates the transcription of a variety of genes that respond to hypoxia conditions (1,2). There are several isoforms of the HIF α subunit (2). Studies have found that HIF-1α and HIF-2α expression is increased in some human cancers (2). HIF-1α has both pro- and anti-proliferative activities, whereas HIF-2α does not possess anti-proliferative activity (2). Therefore, HIF-2α likely plays an important role in tumorigenesis (2,3).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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