BCL2L1 Antibodies

BCL2L1 (BCL2 Like 1) is a Protein Coding gene. Diseases associated with BCL2L1 include T-Cell Leukemia and Follicular Lymphoma. Among its related pathways are Amyotrophic lateral sclerosis (ALS) 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 BCL2.

CUSABIO produces high-quality anti-BCL2L1 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 BCL2L1 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 BCL2L1 antibodies custom service.

BCL2L1 Antibodies Catalog

BCL2L1 Antibodies for Homo sapiens (Human)

BCL2L1 Background

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.

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[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.


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