Bcl-2 homologous antagonist/killer is a protein in humans that is encoded by BAK1 gene. In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2 or its adenovirus homolog E1B 19k protein. Low micromolar levels of zinc ions inhibit the promotion of apoptosis.
The following BAK1 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.
BAK1 Antibodies for Homo sapiens (Human)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA002548GA01HU | BAK1 Antibody |
Human,Mouse,Rat | ELISA,WB,IHC |
CSB-PA886292 | BAK1 Antibody |
Human | ELISA,WB,IHC,IF |
CSB-PA000971 | BAK1 Antibody |
Human,Mouse | WB, IHC, IF, ELISA |
CSB-PA089402 | BAK1 Antibody |
Human | ELISA,WB,IHC |
CSB-PA299203 | BAK1 Antibody |
Human | ELISA,WB |
CSB-RA624111A0HU | BAK1 Recombinant Monoclonal Antibody |
Human | ELISA, WB, IHC, FC, IP |
BAK1 Antibodies for Arabidopsis thaliana (Mouse-ear cress)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA850098XA01DOA | BAK1 Antibody |
Arabidopsis thaliana | ELISA, WB (ensure identification of antigen) |
BAK1 Antibodies for Oryza sativa subsp. indica (Rice)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA295504XA01OFF | BAK1 Antibody |
Oryza sativa subsp. indica (Rice) | ELISA, WB (ensure identification of antigen) |
BAK1 Antibodies for Oryza sativa subsp. japonica (Rice)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA992932XA01OFG | BAK1 Antibody |
Oryza sativa subsp. japonica (Rice) | ELISA, WB (ensure identification of antigen) |
BAK1 Proteins for Arabidopsis thaliana (Mouse-ear cress)
Code | Product Name | Source |
---|---|---|
CSB-YP850098DOA CSB-EP850098DOA CSB-BP850098DOA CSB-MP850098DOA CSB-EP850098DOA-B |
Recombinant Arabidopsis thaliana BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 (BAK1), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
BAK1 Proteins for Mus musculus (Mouse)
Code | Product Name | Source |
---|---|---|
CSB-CF002548MO | Recombinant Mouse Bcl-2 homologous antagonist/killer (Bak1) |
in vitro E.coli expression system |
CSB-YP002548MO1 CSB-EP002548MO1 CSB-BP002548MO1 CSB-MP002548MO1 CSB-EP002548MO1-B |
Recombinant Mouse Bcl-2 homologous antagonist/killer (Bak1), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
BAK1 Proteins for Homo sapiens (Human)
Code | Product Name | Source |
---|---|---|
CSB-CF624111HU | Recombinant Human Bcl-2 homologous antagonist/killer (BAK1) |
in vitro E.coli expression system |
CSB-YP624111HU1 CSB-EP624111HU1 CSB-BP624111HU1 CSB-MP624111HU1 CSB-EP624111HU1-B |
Recombinant Human Bcl-2 homologous antagonist/killer (BAK1), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
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.
[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.