Bcl-2-like protein 1 is a protein in humans that is encoded by BCL2L1 gene. Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.
The following BCL2L1 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.
BCL2L1 Antibodies for Homo sapiens (Human)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA027199GA01HU | BCL2L1 Antibody |
Human,Mouse,Rat | ELISA,WB,IHC |
CSB-MA0026131A0m | BCL2L1 Monoclonal Antibody |
Human | ELISA,WB,IHC |
CSB-PA002613HA01HU | BCL2L1 Antibody |
Human, Mouse | ELISA, WB, IHC, IF |
CSB-PA002613HB01HU | BCL2L1 Antibody, HRP conjugated |
Human | ELISA |
CSB-PA923588 | BCL2L1 (Ab-62) Antibody |
Human,Mouse,Rat | ELISA,WB |
CSB-PA786016 | Phospho-BCL2L1 (Ser62) Antibody |
Human, Mouse, Rat | ELISA, WB, IHC, IF |
CSB-PA000986 | BCL2L1 Antibody |
Human,Mouse,Rat | WB, IHC, IF, ELISA |
CSB-PA000987 | BCL2L1 Antibody |
Human,Mouse,Rat | WB, IHC, ELISA |
CSB-PA040205 | Phospho-BCL2L1 (S62) Antibody |
Human,Mouse,Rat | WB, IHC, ELISA |
CSB-PA040206 | Phospho-BCL2L1 (T47) Antibody |
Human,Mouse,Rat | WB, IHC, IF, ELISA |
CSB-PA040207 | Phospho-BCL2L1 (T115) Antibody |
Human,Mouse,Rat | IHC, ELISA |
CSB-PA040208 | BCL2L1 Antibody |
Human,Mouse,Rat | IHC, ELISA |
CSB-PA080279 | BCL2L1 Antibody |
Human,Mouse,Rat | IHC |
CSB-PA223208 | BCL2L1 Antibody |
Human,Mouse,Rat | ELISA,WB |
CSB-PA315068 | BCL2L1 Antibody |
Human,Mouse,Rat | ELISA,WB |
CSB-RA247982A0HU | BCL2L1 Recombinant Monoclonal Antibody |
Human, Mouse, Rat | ELISA, WB, IHC |
BCL2L1 Proteins for Homo sapiens (Human)
Code | Product Name | Source |
---|---|---|
CSB-EP002613HU | Recombinant Human Bcl-2-like protein 1 (BCL2L1), partial |
E.coli |
CSB-YP002613HU CSB-BP002613HU CSB-MP002613HU CSB-EP002613HU-B |
Recombinant human Bcl-2-like protein 1 |
Yeast Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
BCL2L1 Proteins for Mus musculus (Mouse)
Code | Product Name | Source |
---|---|---|
CSB-CF731050MO | Recombinant Mouse Bcl-2-like protein 1 (Bcl2l1) |
in vitro E.coli expression system |
CSB-YP731050MO1 CSB-EP731050MO1 CSB-BP731050MO1 CSB-MP731050MO1 CSB-EP731050MO1-B |
Recombinant Mouse Bcl-2-like protein 1 (Bcl2l1), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
BCL2L1 Proteins for Rattus norvegicus (Rat)
Code | Product Name | Source |
---|---|---|
CSB-CF002613RA | Recombinant Rat Bcl-2-like protein 1 (Bcl2l1) |
in vitro E.coli expression system |
CSB-YP002613RA1 CSB-EP002613RA1 CSB-BP002613RA1 CSB-MP002613RA1 CSB-EP002613RA1-B |
Recombinant Rat Bcl-2-like protein 1 (Bcl2l1), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
BCL2L1 Proteins for Sus scrofa (Pig)
Code | Product Name | Source |
---|---|---|
CSB-CF002613PI | Recombinant Pig Bcl-2-like protein 1 (BCL2L1) |
in vitro E.coli expression system |
CSB-YP002613PI1 CSB-EP002613PI1 CSB-BP002613PI1 CSB-MP002613PI1 CSB-EP002613PI1-B |
Recombinant Pig Bcl-2-like protein 1 (BCL2L1), partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
BCL2L1 ELISA Kit for Homo sapiens (Human)
Code | Product Name | Sample Types | Sensitivity |
---|---|---|---|
CSB-EL002613HU | Human Bcl-2-like protein 1(BCL2L1) ELISA kit |
serum, plasma, tissue homogenates | 0.156 ng/mL |
BCL2L1 ELISA Kit for Rattus norvegicus (Rat)
Code | Product Name | Sample Types | Sensitivity |
---|---|---|---|
CSB-E13604r | Rat Bcl-2-like protein 1(Bcl2-L-1/Bcl-X)ELISA Kit |
serum, plasma, tissue homogenates, cell lysates | 11.72 pg/mL |
Because of alternative splicing of BCL2L1 mRNA, the BCL2L1 gene encodes two different protein products: a cytoprotective factor of 233 residues (BCL-XL) and a smaller polypeptide (170 residues) that exerts BCL-XL-antagonizing functions (BCL-XS) [1].
Like other BCL-2 proteins, BCL-XL contains four distinct BCL-2 homology (BH) domains (BH1-BH4) as well as a transmembrane region that contributes to its localization to the mitochondrial outer membrane (MOM), the endoplasmic reticulum (ER), and the nuclear envelope [1][2][3]. However, BCL-XS lacks both the BH1 and BH2 domains [1][4]. BCL-XL is mainly expressed in most physiological conditions [5], but BCL-XS often predominates in situations of developmental and pharmacological cell death [6][7].
Similar to BCL-2, BCL-XL exerts the anti-apoptotic function or prosurvival role. BCL-XL sequesters its proapoptotic counterparts BAX and BAK in inhibitory interactions, preventing the formation of lethal pores in the mitochondrial outer membrane (MOM), as well as to multiple BH3-only proteins such as BAD, thus blocking apical proapoptotic signals [8].
Besides, BCL-XL has been suggested to execute cytoprotective functions by detaining a cytosolic pool of the pro-apoptotic transcription factor p53 [9] and by binding to the voltage-dependent anion channel 1 (VDAC1), thereby repressing the mitochondrial permeability transition (MPT) [10][11]. In particular, BCL-XL has been shown to regulate multiple pathophysiological processes, including mitochondrial ATP synthesis [12], protein acetylation [13], autophagy, and mitosis.
[1] L. H. Boise, M. Gonzalez-Garcia, et al. bcl-x, A bcl-2-related gene that functions as a dominant regulator of apoptotic cell death [J]. Cell, vol. 74, no. 4, pp. 597-608, 1993.
[2] F. W. H. Ng, M. et al. p28 Bap31, a Bcl-2/Bcl-X(L)- and procaspase-8-associated protein in the endoplasmic reticulum [J]. Journal of Cell Biology, vol. 139, no. 2, pp. 327-338, 1997.
[3] E. Schmitt, M. Beauchemin, et al. Nuclear colocalization and interaction between bcl-xL and cdk1(cdc2) during G2/M cell-cycle checkpoint [J]. Oncogene, vol. 26, no. 40, pp. 5851-5865, 2007.
[4] W. Fang, J. J. Rivard, et al. Cloning and molecular characterization of mouse bcl-x in B and T lymphocytes [J]. Journal of Immunology, vol. 153, no. 10, pp. 4388-4398, 1994.
[5] M. Gonzalez-Garcia, et al. bcl-x(L) is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria [J]. Development, vol. 120, no. 10, pp. 3033-3042, 1994.
[6] K. Heermeier, M. Benedict, et al. Bax and Bcl-xs are induced at the onset of apoptosis in involuting mammary epithelial cells [J].of Development, vol. 56, no. 1-2, pp. 197-207, 1996.
[7] S. Willimott, T. Merriam, et al. Apoptosis induces Bcl-XS and cleaved Bcl-xL in chronic lymphocytic leukaemia [J]. Biochemical and Biophysical Research Communications, vol. 405, no. 3, pp. 480-485, 2011.
[8] E. Yang, J. Zha, et al. Bad, a heterodimeric partner for Bcl-x(L), and Bcl-2, displaces Bax and promotes cell death [J]. Cell, vol. 80, no. 2, pp. 285–291, 1995.
[9] M. Mihara, S. Erster, et al. p53 has a direct apoptogenic role at the mitochondria [J]. Molecular Cell, vol. 11, no. 3, pp. 577-590, 2003.
[10] S. Shimizu, Y. Shinohara, et al. Bax and Bcl-x(L) independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator [J]. Oncogene, vol. 19, no. 38, pp. 4309-4318, 2000.
[11] M. G. Vander Heiden, et al. Bcl-xL promotes the open configuration of the voltage-dependent anion channel and metabolite passage through the outer mitochondrial membrane [J]. The Journal of Biological Chemistry, vol. 276, no. 22, pp. 19414-19419, 2001.
[12] K. N. Alavian, H. Li, L. Collis et al. Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase [J]. Nat Cell Biol, vol. 13, pp. 1224-1233, 2011.
[13] C. H. Yi et al. Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival [J]. Cell, vol. 146, pp. 607-620, 2011.