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Informacje o tej pozycji
Quality Level
biological source
rabbit
conjugate
unconjugated
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human
technique(s)
ChIP: suitable, electrophoretic mobility shift assay: suitable, western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... GABPA(2551)
General description
Immunogen
Application
Western Blotting Analysis: A representative lot detected GABPA (NRF-2alpha) in U2OS cell lysates (Gleyzer, N., and Scarpulla, R.C. (2011). J. Biol. Chem. 286(46):39715-39725; Gleyzer, N., and Scarpulla, R.C. (2013). J. Biol. Chem. 288(12):8004-8015).
Electrophoretic Mobility Shift Assay (EMSA) Analysis: A representative lot caused a supershift of GABPA (NRF-2alpha)-DNA complex in EMSA using recombinant GABPA or heparin agarose-purified HeLa nuclear extract and radiolabeled synthetic oligonucleotides corresponding to cytochrome oxidase subunit IV, hTFB1M, or hTFB2M promoter sequence with GABPA recognition sites (Gleyzer, N., et al. (2005). Mol Cell Biol. 2005 Feb;25(4):1354-66).
Electrophoretic Mobility Shift Assay (EMSA) Analysis: A representative lot caused a supershift of GABPA (NRF-2alpha)-DNA complex in EMSA using in vitro translated GABPA and radiolabeled cytochrome oxidase subunit IV promoter fragment containing tandem GABPA recognition sites (Vercauteren, K., et al. (2008). J Biol Chem. 283(18):12102-12111).
Immunoprecipitation Analysis: A representative lot immunoprecipitated GABPA (NRF-2alpha)-PRC complex from human embryonic kidney 293FT cell lysate (Vercauteren, K., et al. (2008). J Biol Chem. 283(18):12102-12111).
Analysis Note
Western Blotting Analysis: A 1:500 dilution of this antibody detected NRF2a/GABPA in 10 µg of HeLa cell lysate.
Other Notes
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Klasa składowania
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Powiązane treści
A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.
Numer pozycji handlu globalnego
| SKU | NUMER GTIN |
|---|---|
| ABE1047 | 04055977181562 |