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Bax inhibitor peptide, negative control
Discontinued ProductBax inhibitor peptide, negative control (Cat. No. 1787) has been withdrawn from sale for commercial reasons.
Negative control peptide for the Bax inhibitor peptide V5, which inhibits Bax translocation to mitochondria and Bax-mediated apoptosis in vitro.
Active Analog V5 also available.
|Storage||Desiccate at -20°C|
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
References are publications that support the biological activity of the product.
Yoshida et al (2004) Bax-inhibiting peptide derived from mouse and rat Ku70. Biochem.Biophys.Res.Commun. 321 961 PMID: 15358121
Sawatzky et al (2006) The involvement of the apoptosis-modulating proteins ERK 1/2, Bcl-xL and Bax in the resolution of acute inflammation in vivo. Am.J.Pathol. 168 33 PMID: 16400007
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Keywords: Bax inhibitor peptide, negative control, Bax inhibitor peptide, negative control supplier, Negative, control, peptide, 5, 1786, Bax, Bcl-XL, Mcl-1, Bcl-2, Family, 1787, Tocris Bioscience
1 Citation for Bax inhibitor peptide, negative control
Citations are publications that use Tocris products. Selected citations for Bax inhibitor peptide, negative control include:
Lee et al (2010) Angiotensin-II-induced apoptosis requires regulation of nucleolin and Bcl-xL by SHP-2 in primary lung endothelial cells. J Cell Sci 123 1634 PMID: 20406888
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Literature in this Area
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Parkinson's disease (PD) causes chronic disability and is the second most common neurodegenerative condition. This poster outlines the neurobiology of the disease, as well as highlighting current therapeutic treatments for symptomatic PD, and emerging therapeutic strategies to delay PD onset and progression.
Programmed Cell Death Poster
There are two currently recognized forms of programmed cell death: apoptosis and necroptosis. This poster summarizes the signaling pathways involved in apoptosis, necroptosis and cell survival following death receptor activation, and highlights the influence of the molecular switch, cFLIP, on cell fate.