BAX Research Reagents

Apoptosis regulator BAX is a protein in humans that is encoded by BAX gene. Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.

The following BAX reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

BAX Antibodies

BAX Antibodies for Homo sapiens (Human)

BAX Antibodies for Escherichia coli (strain K12)

BAX Proteins

BAX Proteins for Escherichia coli (strain K12)

BAX Proteins for Rattus norvegicus (Rat)

BAX Proteins for Bos taurus (Bovine)

BAX ELISA Kit

BAX ELISA Kit for Homo sapiens (Human)

BAX ELISA Kit for Rattus norvegicus (Rat)

BAX Background

As a member of the Bax subfamily that belongs to the Bcl-2 family of proteins, Bcl-2-associated X protein (BAX) is a pro-apoptotic protein encoded by the BAX gene [1]. BAX contains conserved Bcl-2 homology domains (BH1, BH2, BH3, and BH4)and a hydrophobic region at the C-terminal ends that are believed to serve as a membrane-spanning domain [1][2]. BAX expression is regulated by the tumor suppressor P53, and it is involved in P53-mediated apoptosis. Although the subcellular localization of Bax has not been known, Bax has been suggested to colocalize within the same subcellular compartments as Bcl-2 due to the presence of its putative C-terminal transmembrane segment and its ability to dimerize with Bcl-2 [3]. A majority of BAX proteins are found in the cytosol before apoptosis induction [4][5]. Upon the induction of apoptotic signals, BAX undergoes a conformation alteration, making itself translocate from the cytosol to mitochondria [4][5] where it participates in mitochondrial disruption and the release of cytochrome c. The loss of cytochrome c from mitochondria disables energy production, and cytosolic cytochrome c triggers a proteolytic cascade that dismantles the cell, namely apoptosis. Regulating the insertion of BAX into the mitochondrial outer membrane can regulate apoptosis [6][7]. Extensive mutagenesis studies have shown that the docking of BAX to mitochondria is dependent on its C-terminal sequence. The conformational change of the BAX C-terminus exposes the hydrophobic BH3 binding pocket that is involved in dimer formation, thus modulating the subcellular location of BAX and apoptosis [8]. Studies have proved that drugs such as ABT737 and a BH3 mimetic, that activate BAX, are the potential to be anticancer therapies by inducing apoptosis in cancer cells [9].

[1] Adams J.M., Cory S. The Bcl-2 protein family [J]. Science. 1998; 281: 1322-1326.
[2] Gross A., McDonnell J.M., et al. BCL-2 family members and the mitochondria in apoptosis [J]. Genes Dev. 1999; 13: 1899-1911.
[3] Oltvai Z N, Milliman C L, et al. Bcl-2 Heterodimerizes in Vivo With a Conserved Homolog, Bax, That Accelerates Programmed Cell Death [J]. Cell. 1993;74:609-619.
[4] Hsu Y.T., Wolter K.G., et al. Cytosol-to-membrane redistribution of Bax and Bcl-XL during apoptosis [J]. Proc. Natl. Acad. Sci. USA. 1997; 94: 3668-3672.
[5] Wolter K.G., Hsu Y.T., et al. Movement of Bax from the cytosol to mitochondria during apoptosis [J].J. Cell Biol. 1997; 139: 1281-1292.
[6] Goping I.S., Gross A., et al. Regulated targeting of BAX to mitochondria [J]. J. Cell Biol. 1998; 143: 207-215.
[7] Gross A., Jockel J., et al. Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis [J]. EMBO J. 1998; 17: 3878-3885.
[8] Nechushtan A., Smith C.L., et al. Conformation of the Bax C-terminus regulates subcellular location and cell death [J]. EMBO J. 1999; 18: 2330-2341.
[9] Westphal, D, Kluck, RM, et al. Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis [J]. Cell Death & Differentiation. February 2014, 21 (2): 196-205.

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