BCL2L1 Proteins

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.

The following recombinant BCL2L1 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 BCL2L1 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 BCL2L1 proteins custom service will be also offered.

BCL2L1 Proteins Catalog

BCL2L1 Proteins for Homo sapiens (Human)

BCL2L1 Proteins for Mus musculus (Mouse)

BCL2L1 Proteins for Rattus norvegicus (Rat)

BCL2L1 Proteins for Sus scrofa (Pig)

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.

[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.

Newsletters

Get all the latest information on Events, Sales and Offers. Sign up for newsletter today.

© 2007-2020 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1