BCL2 Proteins

BCL2 (BCL2 Apoptosis Regulator) is a Protein Coding gene. Diseases associated with BCL2 include High Grade B-Cell Lymphoma With Myc And/ Or Bcl2 And/Or Bcl6 Rearrangement and Follicular Lymphoma 1. Among its related pathways are Direct p53 effectors and Amyotrophic lateral sclerosis (ALS). Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and identical protein binding. An important paralog of this gene is BCL2L1.

The following recombinant BCL2 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 BCL2 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 BCL2 proteins custom service will be also offered.

BCL2 Proteins Catalog

BCL2 Proteins for Mus musculus (Mouse)

BCL2 Proteins for Bos taurus (Bovine)

BCL2 Proteins for Gallus gallus (Chicken)

BCL2 Proteins for Canis lupus familiaris (Dog) (Canis familiaris)

BCL2 Proteins for Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

BCL2 Proteins for Rattus norvegicus (Rat)

BCL2 Proteins for Homo sapiens (Human)

BCL2 Background

BCL2 is a proto-oncogene that was discovered at the chromosomal breakpoint of t(14;18) bearing human B-cell lymphomas [1]. The BCL2 gene encodes Bcl-2 (B-cell lymphoma 2), a multiple-domain anti-apoptotic protein. Pablo Mozas et al. found that in chronic lymphocytic leukemia (CLL) cells, excess of BCL2 and other anti-apoptotic proteins sequesters pro-apoptotic molecules such as BIM and BID, thus blocking the activation of BAK or BAX and subsequent apoptosis [2]. Many cancer cells, including most B cell-derived lymphomas, colorectal adenocarcinomas, and undifferentiated nasopharyngeal cancers have been detected Bcl-2 overexpression [3]. The unique oncogenic role of Bcl-2 has largely assumed its extending cell survival by inhibiting a variety of apoptotic deaths. Bcl-2 has been also involved in the resistance of many cancers to treatment with radiation and chemotherapeutic agents [4][5]. The functional ablation of Bcl-2 or other antiapoptotic proteins, such as Bcl-xL, could either induce apoptosis in cancer cells or sensitize these cells for chemotherapy. Therefore, Bcl-2 represents a target for the treatment of cancers, especially those in which Bcl-2 is overexpressed and for which traditional therapy has failed [3][6]. Mutations in the hydrophobic groove region within Bcl-2 protein have been shown to abolish its antiapoptotic activity and disrupt heterodimerization with other family members [6]. Yin X M et al. also proved that BH1 and BH2 domains of Bcl-2 are indispensable for apoptotic repression and heterodimerization With Bax [7].

[1] Tsujimoto Y, Finger LR, et al. Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation [J]. Science. 1984 Nov 30; 226(4678):1097-9.
[2] Valentín Ortíz-Maldonado, Pablo Mozas, et al. The biology behind B-cell lymphoma 2 as a target in chronic lymphocytic leukemia [J]. Ther Adv Hematol. 2016 Dec; 7(6): 321-329.
[3] Berghella A M, Pellegrini P, et al. Bcl-2 and Drugs Used in the Treatment of Cancer: New Strategies of Biotherapy Which Should Not Be Underestimated [J]. Cancer Biother Radiopharm, 1998, 13:225-236.
[4] Reed J C. Mechanisms of Apoptosis Avoidance in Cancer [J]. Curr Opin Oncol,1999, 11:68-75.
[5] Kusenda J Bcl-2 family proteins and leukemia [J]. Neoplasma (Bratisl), 1998, 45:117-122.
[6] Nicholson D W From Bench to Clinic With Apoptosis-Based Therapeutic Agents [J]. Nature (London) 2000, 407:810-816.
[7] Yin X M, Oltvai Z N, et al. BH1 and BH2 Domains of Bcl-2 Are Required for Inhibition of Apoptosis and Heterodimerization With Bax [J]. Nature (London) 1994, 369:321-323.

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