BAX Antibodies

BAX (BCL2 Associated X, Apoptosis Regulator) is a Protein Coding gene. Diseases associated with BAX include Colorectal Cancer and Precursor T-Cell Acute Lymphoblastic Leukemia. Among its related pathways are Direct p53 effectors and NGF Pathway. Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and protein heterodimerization activity. An important paralog of this gene is MCL1.

CUSABIO produces high-quality anti-BAX antibodies (includes polyclonal antibodies, monoclonal antibodies, recombinant antibodies) in house with strict quality control. And they can help you discover more in your research.
These BAX antibodies are validated in multiple tissues with various applications and covering a broad range of life science research and drug development. They are featured with high specificity, multiple epitopes recognition, and wide species reactivity. Moreover, CUSABIO provides various options on sizes, excellent technical support and BAX antibodies custom service.

BAX Antibodies Catalog

BAX Antibodies for Homo sapiens (Human)

BAX Antibodies for Escherichia coli (strain K12)

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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