Category: Proteins & Peptides

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PUMA peptide

Reference: GTX29646

Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 upregulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse (1-3). PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMA-a and PUMA-b (1). PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.

EndoG peptide

Reference: GTX29648

The fragmentation of nuclear DNA is a hallmark of apoptotic cell death. The activities of caspase and nuclease are involved in the DNA fragmentation. Caspase-activated deoxyribonuclease (CAD), also termed DNA fragmentation factor (DFF4), is one such nuclease, and is capable of inducing DNA fragmentation and chromatin condensation after cleavage by caspase-3 of its inhibitor ICAD/DFF45. Caspase and CAD independent DNA fragmentation also exists. Recent studies demonstrated that another nuclease, endonuclease G (endoG), is specifically activated by apoptotic stimuli and is able to induce nucleosomal fragmentation of DNA independently of caspase and DFF/CAD (1,2). EndoG is a mitochondrion-specific nuclease that translocates to the nucleus and cleaves chromatin DNA during apoptosis. The homologue of mammalian EndoG is the first mitochondrial protein identified to be involved in apoptosis in C. elegans (2). EndooG also cleaves DNA in vitro (4).

CARD9 peptide

Reference: GTX29650

Apoptosis is related to many diseases and development. Cell death signals are transduced by death domain (DD), death effector domain (DED), and caspase recruitment domain (CARD) containing molecules. CARD containing proteins include some caspases, Apaf-1, CARD4, IAPs, RICK, ARC, RAIDD, BCL-1, and ASC. A novel CARD-containing protein was recently identified and designated CARD9, which interacts with the CARD activation domain of BCL-1 (1). CARD9 associates with BCL-1 and forms a complex within cells. CARD9 induces apoptosis and activates NF-kB. CARD9 is an upstream activator of BCL-1 and NF-kB signaling.

ARTS peptide

Reference: GTX29652

Apoptosis is related to many diseases and development. Mitochondrial proteins, such as cytochrome c, Apaf-1, and AIF play important role in apoptosis. A novel mitochondrial septin-like protein was identified recently and designated ARTS for apoptosis related protein in TGF-b signaling pathway (1). ARTS that is encoded by the human septin H5/PNUTL2/CDCrel2b gene (1-4) is located to mitochondria and translocates to the nucleus when apoptosis occurs. ARTS is expressed in many tissues. It enhances cell death induced by TGF-b and, to a lesser extent, by other apoptotic agents, such as TNF-a and Fas ligand.

BMF peptide

Reference: GTX29654

Apoptosis is related to many diseases and development. Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain is a potent death domain. BH3-only proteins, including Bad, Bid, Bik, Hrk, Bim, Noxa, and PUMA, form a growing subclass of the Bcl-2 family. A novel BH3-only protein was recently identified in human and mouse and designated Bmf (for Bcl-2-modifing factor) (1). The BH3 domain in Bmf is required both for binding to Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf associates with the dynein light chain 2 (DLC2) component of the myosin V motors and is sequestered by the cell's actin cytoskeleton. Disruption of the actin cytoskeleton, either by depolymerization of actin filaments or by detachment of cells from the extracellular matrix, triggers release and activation of Bmf, initiating the downstream apoptotic program (1,2). Bmf is constitutively expressed in many tissues (1,2).

BMF peptide

Reference: GTX29656

Apoptosis is related to many diseases and development. Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain is a potent death domain. BH3-only proteins, including Bad, Bid, Bik, Hrk, Bim, Noxa, and PUMA, form a growing subclass of the Bcl-2 family. A novel BH3-only protein was recently identified in human and mouse and designated Bmf (for Bcl-2-modifing factor) (1). The BH3 domain in Bmf is required both for binding to Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf associates with the dynein light chain 2 (DLC2) component of the myosin V motors and is sequestered by the cell's actin cytoskeleton. Disruption of the actin cytoskeleton, either by depolymerization of actin filaments or by detachment of cells from the extracellular matrix, triggers release and activation of Bmf, initiating the downstream apoptotic program (1,2). Bmf is constitutively expressed in many tissues (1,2).

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