BCL2 Research Reagents

Apoptosis regulator Bcl-2is a protein in humans that is encoded by BCL2 gene. Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release.

The following BCL2 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

BCL2 Antibodies

BCL2 Antibodies for Mus musculus (Mouse)

BCL2 Antibodies for Homo sapiens (Human)

BCL2 Proteins

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 ELISA Kit

BCL2 ELISA Kit for Homo sapiens (Human)

BCL2 ELISA Kit for Mus musculus (Mouse)

BCL2 ELISA Kit for Rattus norvegicus (Rat)

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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