BAK1 Proteins

BAK1 (BCL2 Antagonist/Killer 1) is a Protein Coding gene. Diseases associated with BAK1 include Keratoacanthoma and Indolent B-Cell Non-Hodgkin Lymphoma. Among its related pathways are Direct p53 effectors and CDK-mediated phosphorylation and removal of Cdc6. Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and protein heterodimerization activity. An important paralog of this gene is BCL2L1.

The following recombinant BAK1 proteins are manufactured in house under a complete QC system by CUSABIO. They are expressed by Yeast, E.coli, Baculovirus, Mammalian cell, In Vivo Biotinylation in E.coli. Highlights of these recombinant BAK1 proteins as follow:
High purity, Low endotoxin, Multiple Tags, Animal-free, Wide applications (Cell assay, Protein-protein interaction, Drug-related studies, Enzymatic activity in vitro, Protein structure analysis, etc.)
In addition, various options on sizes, excellent technical support, and recombinant BAK1 proteins custom service will be also offered.

BAK1 Proteins Catalog

BAK1 Proteins for Arabidopsis thaliana (Mouse-ear cress)

BAK1 Proteins for Mus musculus (Mouse)

BAK1 Proteins for Homo sapiens (Human)

BAK1 Background

Bcl-2 homologous antagonist/killer (BAK) is a protein in humans that is encoded by the BAK1 gene on chromosome 6 [1]. BAK is a member of the Bcl-2 family and contains four Bcl-2 homology (BH) domains: BH1, BH2, BH3, and BH4. In healthy mammalian cells, BAK localizes primarily to the mitochondrial outer membrane (MOM) but keeps in an inactive monomer form. BAK is activated by BH3-only proteins such as BAD under apoptotic stimulation. The activation of pro-apoptotic effector protein BAK induces its oligomerization into proteolipid pores in the MOM [2][3], inducing the MOM permeabilization and cytochrome c release that ultimately triggers apoptosis. Evidence has shown that BAK can form heterogeneous dimers with Bcl-2 or Bcl-xL to inhibit their anti-apoptotic functions [4]. The BAK deficiency was directly responsible for the arrest in cytochrome c release. This capability was normalized to the BAK-deficient cells by the insertion of recombinant BAK into purified mitochondria from these cells [5]. Current evidence indicated that deficiency of BAK expression is closely associated with the occurrence and development of tumors [6], but BAK1 overexpression contributes to neurodegenerative and autoimmune diseases [7]. Gottlieb B et al. found that different BAK1 variants can exist in both diseased and non-diseased abdominal aortic aneurysm (AAA) tissues compared to matching blood samples in the research of studying the role of genetics in AAA [8]. Pataer et al. reported that adenoviral-mediated overexpression of BAK could induce obvious apoptosis in lung and breast cancer cells, which provided a novel therapeutic strategy for cancer treatment [9]. Moreover, many kinds of tumor therapeutic drugs such as perillyl alcohol and γ-interferon, exert their functions through up-regulating BAK expression [10].

[1] Chittenden T, Harrington EA, et al. Induction of apoptosis by the Bcl-2 homologue Bak [J]. Nature. 374 (6524): 733-6.
[2] Pang YP, Dai H, et al. Bak conformational changes induced by ligand binding: insight into BH3 domain binding and Bak homo-oligomerization [J]. Sci Rep 2012; 2: 257.
[3] Ma S, Hockings C, et al. Assembly of the Bak apoptotic pore: A critical role for the Bak alpha6 helix in the multimerization of homodimers during apoptosis [J]. The Journal of biological chemistry 2013; 288: 26027-26038.
[4] Degli Esposti M, Dive C. Mitochondrial membrane permeabilization by Bax/BAK [J]. Biochem Biophys Res Commun. 2003, 304: 455-461.
[5] Wang GQ, Gastman BR, et al. A role for mitochondrial Bak in the apoptotic response to anticancer drugs [J]. J Biol Chem. 2001, 276: 34307-34317.
[6] Rosen K, Rak J, et al. Downregulation of the pro-apoptotic protein BAK is required for the ras-induced transformation of intestinal epithelial cells [J].Curr Biol. 1998, 8: 1331-1334.
[7] Cartron PF, Petit E, et al. Metaxins 1 and 2, two proteins of the mitochondrial protein sorting and assembly machinery, are essential for Bak activation during TNF alpha triggered apoptosis [J]. Cellular Signalling. 2014, 26 (9): 1928-34.
[8] Gottlieb B, Chalifour LE, et al. BAK1 gene variation and abdominal aortic aneurysms [J]. Human Mutation. 2009, 30 (7): 1043-7.
[9] Pearson AS, Spitz FR, et al. Up-regulation of the pro-apoptotic mediators Bax and BAK after adenovirus-mediated p53 gene transfer in lung cancer cells [J]. Clin Cancer Res. 2000, 6: 887-890.
[10] Ahn EY, Pan G, et al. IFN-gamma upregulates apoptosis-related molecules and enhances Fas-mediated apoptosis in human cholangiocarcinoma [J]. Int J Cancer. 2002, 100: 445-451.


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