Overview
Available Bio-Plex Pro™ Apoptosis Assays
| Apoptosis Panel 1 | Apoptosis Panel 2 | Apoptosis Panel 3 | |||
| Analyte | Bead Region | Analyte | Bead Region | Analyte | Bead Region |
| Bak | 74 | Bad | 74 | Active caspase-3 | 57 |
| Bax | 27 | Bax/Bcl-2 dimer | 42 | Bcl-xL/Bak dimer | 47 |
| Lamin B, intact and 45 kD |
14 | Bcl-xL | 22 | Mcl-1/Bak dimer | 54 |
| Smac | 19 | Bim | 12 | Survivin | 20 |
| Mcl-1 | 18 | ||||
Apoptosis Analyte Descriptions
| Analyte | Analyte Descriptions | Apoptotic Action | Apoptotic Cell |
| Bak | Bcl-homologous antagonist/killer is a pro-apoptotic member of the Bcl-2 family. In healthy cells, it is integrated in the mitochondrial outer membrane. Upon apoptotic stimuli, Bak forms oligomer channels in the mitochondrial membrane for cytochrome C release. This activity is regulated by forming a complex with anti-apoptotic Mcl-1 and Bcl-xL. | Pro-apoptotic | Mitochondrial membrane |
| Bax | Bcl-2 associated protein X is a pro-apoptotic member of the Bcl-2 family. In healthy cells, it is found as a monomer in the cytosol, but upon apoptotic stimuli, it translocates to the mitochondrial outer membrane and forms large oligomeric complexes. There it interacts with pore proteins to enable cytochrome C release into the cytosol and initiate the caspase activation pathway for apoptosis. Bax may cycle to the mitochondrial membrane and dimerize with Bcl-xL. | Pro-apoptotic | Moves to the mitochondrial membrane |
| Lamin B, intact and 45 kD |
Nuclear lamins are proteins of intermediate filament type located at the outer rim of the nucleus. They consist of two types of polypeptides, lamin A and lamin B. Lamin B consists of B1 and B2 subtypes. Lamins mechanically stabilize the cell nucleus and also play a role in DNA replication and chromatin organization. Lamin B is cleaved by caspase-3 and caspase-6 during the early phases of apoptosis (up to 90 min) before DNA fragmentation. Detection of cytoplasmic dissociated lamin B indicates cell apoptosis. | Early indicator of apoptosis | Cytosol |
| Smac | Second mitochondria-derived activator of caspase is a dimeric mitochondrial protein synthesized in the cytoplasm as a 239 amino acid precursor protein, with 55 amino acids at the N-terminus serving as a mitochondrial-targeting sequence. Under apoptotic stimuli, it is proteolytically cleaved to a 23 kD active form and released into the cytosol together with cytochrome C, where it reverses IAP inhibition of caspase-9, allowing caspase-9 to activate the caspase cascade. | Pro-apoptotic | Cytosol |
| Bad | Bcl-2-associated death promoter is a pro-apoptotic, BH3-only binding domain member of the Bcl-2 family. BH3-only proteins connect apoptotic death signals to the activation of Bax and Bak, which control mitochondrial membrane disruption and apoptosis. Phosphorylated BAD (pBAD) is typically bound to the cytosolic protein 14-3-3, and is thus sequestered away from the mitochondria. Dephosphorylation results in the release of cytosolic (free) BAD, which binds to and inhibits the pro-survival activity of Bcl-2 family proteins at the mitochondrial membrane. | Pro-apoptotic | Cytosol (free) |
| Bax/Bcl-2 dimer | B-cell lymphoma-2 is an anti-apoptotic protein that resides on the outer mitochondrial membrane. When bound to Bax as a heterodimer, it inhibits permeability of the mitochondrial membrane, preventing release of cytochrome C. | Anti-apoptotic | Mitochondrial membrane; decreased with apoptosis |
| Bcl-xL | B-cell lymphoma-extra large is an anti-apoptotic member of the Bcl-2 family found in the outer mitochondrial membrane. Heterodimerization with pro-apoptotic proteins (especially Bak) inhibits apoptosis by preventing release of cytochrome C. | Anti-apoptotic | Mitochondrial membrane |
| Bim | Bcl-2-interacting mediator of cell death is a pro-apoptotic protein belonging to the BH3-only group of the Bcl-2 family. Bim binds and antagonizes pro-survival members of the Bcl-2 family such as Mcl-1, Bcl-xL, and Bcl-2. Three prominent isoforms are generated by alternative splicing: Bim-S, Bim-L, and Bim-EL. Each isoform has the ability to induce apoptosis. | Pro-apoptotic | Cytosol or mitochodrial membrane if dimerized |
| Mcl-1 | Induced myeloid leukemia cell differentiation protein-1 is an anti-apoptotic member of the Bcl-2 family. Heterodimerization with pro-apoptotic proteins (especially Bak) inhibits apoptosis. While Mcl-1 may not be as potent a protector against apoptosis as Bcl-2, it does appear to be the main anti-apoptotic protein in some cell types, including neutrophils. | Anti-apoptotic | Mainly mitochondrial membrane, some in cytosol |
| Active Caspase-3 | Cysteinyl aspartyl protease-3 belongs to the peptidase C14A enzyme family and is known to play an important role in the apoptotic cascade. The active enzyme is formed by cleavage of the inactive 32 kD pro-enzyme into the p17 and p12 subunits. Two of each subunit noncovalently heterodimerize, giving the final enzyme two catalytic sites. Active caspase-3 cleaves and activates other caspases and is a primary regulator of apoptotic-associated proteolysis. | Pro-apoptotic | Cytosol (high levels) |
| Bcl-xL/Bak dimer | Anti-apoptotic Bcl-xL heterodimerizes with Bak at the mitochondrial outer membrane and inhibits permeability of the mitochondrial membrane, preventing release of cytochrome C. During apoptosis BH3-only proteins, such as Bim and Bad, will bind to Bcl-xL and cause Bak to be released. Upon release, Bak will oligomerize creating pores in the mitochondrial membrane. | Anti-apoptotic | Mitochondrial membrane; decreased with apoptosis |
| Mcl-1/Bak dimer | Anti-apoptotic Mcl-1 heterodimerzes with Bax and Bak at the mitochondrial outer membrane to prevent their activation, thus inhibiting cytochrome C release from the mitochondria. | Anti-apoptotic | Mitochondria; decreased with apoptosis |
| Survivin | Survivin is a 16 kD member of the Inhibitor of Apoptosis (IAP) family, which also plays a role in chromosome segregation and cytokinesis. The anti-apoptotic function of survivin comes from its ability to inhibit the activation of caspases-3 and -7. Survivin is found to be upregulated in various tumors. | Anti-apoptotic | Cytosol/nucleus |
Apoptosis Signaling Pathway
Apoptosis is induced by at least two distinct signaling pathways, extrinsic and intrinsic. The extrinsic pathway is triggered by signaling through death receptors such as Fas, followed by downstream activation of caspase-8 and caspase-3. The intrinsic pathway is triggered by cytotoxic stress, which leads to translocation of Bcl-2 family proteins, Bax and Bak, to the mitochondrial membrane. Oligomerization of Bax and Bak causes release of cytochrome C into the cytosol, which promotes apoptosome formation, caspase activation, degradation of nuclear Lamin B, and cell death. Pro-apoptotic proteins included in the panels (
); Anti-apoptotic proteins included in the panels (); Proteins involved in apoptosis but not included in the panels ().
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