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Catalog Number: (200061-588)
Supplier: Enzo Life Sciences
Description: The caspases are a family of cysteine proteases that cleave after certain aspartate residues, and are primarily recognized as mediators of apoptosis. caspases are synthesized as inactive zymogens that can be cleaved to form active enzymes following the induction of apoptosis by stress or death receptors. Initiator caspases (e.g. caspase-8 and -10) are activated by dimerization of the zymogen on a dedicated adaptor protein. These activated initiator caspases in-turn cleave downstream effector or executioner caspases (e.g. caspase-3, -6, and -7) in a cascade-like manner, which cleave key cellular proteins that lead to the morphological changes associated with apoptotic cell death.


Catalog Number: (10362-738)
Supplier: Bioss
Description: Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Could be involved in regulating NF-kappa-B activation and apoptosis. Is a potent inhibitory factor for osteoclast differentiation. Involved in protein degradation via the ubiquitin-proteasome system and plays a critical role in muscle atrophy. May act by anchoring ubiquitinylated proteins to the proteasome, playing a critical role in protein degradation.


Catalog Number: (10362-740)
Supplier: Bioss
Description: Inhibits NF-kappa-B activation triggered by overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent manner. Overexpression sensitizes cells to TNF-induced apoptosis. Could be involved in regulating NF-kappa-B activation and apoptosis. Is a potent inhibitory factor for osteoclast differentiation. Involved in protein degradation via the ubiquitin-proteasome system and plays a critical role in muscle atrophy. May act by anchoring ubiquitinylated proteins to the proteasome, playing a critical role in protein degradation.


Supplier: Adipogen
Description: Potent and cell permeable p38 MAP kinase inhibitor. Apoptosis inducer. Inhibits p38alpha and beta, but not gamma and delta isoforms. Does not inhibit ERK2 or other members of the MAP kinase family or their upstream activators. JNK activator. Autophagic vacuole inducer

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Catalog Number: (10328-322)
Supplier: Bioss
Description: Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.


Catalog Number: (76119-572)
Supplier: Bioss
Description: TID1 is a human homolog of the Drosophila tumor suppressor lethal tumerous imaginal discs and encodes two mitochondrial matrix localized splice variants of human Tid1 designated hTid1S and hTid1L. These proteins are the conserved members of the DnaJ family of proteins which act as cochaperons for mitochondrial Hsp70. They contain a conserved tetrahedrical J domain which binds to Hsp70 chaperones and activates their ATPase activity. Expression of hTid1L increases apoptosis induced by DNA damaging agents as mitomycin C and TNF alpha. A J domain mutant of hTid1L can dominantly suppress apoptosis and in sharp contrast the J domain mutant of hTid1S increases apoptosis. Expression of hTid1S and hTid1L affects cytochrome c release from the mitochondria and caspase 3 activation, while activation of caspase 8 is unaffected. It is strongly suggested that these two splice variants exert their anti and pro apoptotic effects through discrete substrates and activities. Hence the relative abundance of these proteins or their substrates may allow the mitochondria to dampen or enhance the apoptotic signals.


Catalog Number: (76119-574)
Supplier: Bioss
Description: TID1 is a human homolog of the Drosophila tumor suppressor lethal tumerous imaginal discs and encodes two mitochondrial matrix localized splice variants of human Tid1 designated hTid1S and hTid1L. These proteins are the conserved members of the DnaJ family of proteins which act as cochaperons for mitochondrial Hsp70. They contain a conserved tetrahedrical J domain which binds to Hsp70 chaperones and activates their ATPase activity. Expression of hTid1L increases apoptosis induced by DNA damaging agents as mitomycin C and TNF alpha. A J domain mutant of hTid1L can dominantly suppress apoptosis and in sharp contrast the J domain mutant of hTid1S increases apoptosis. Expression of hTid1S and hTid1L affects cytochrome c release from the mitochondria and caspase 3 activation, while activation of caspase 8 is unaffected. It is strongly suggested that these two splice variants exert their anti and pro apoptotic effects through discrete substrates and activities. Hence the relative abundance of these proteins or their substrates may allow the mitochondria to dampen or enhance the apoptotic signals.


Catalog Number: (89154-326)
Supplier: Enzo Life Sciences
Description: The human intracellular serpin proteinase inhibitor 9 (PI9) is the only human protein able to inhibit the activity of the serine protease granzyme B. Granzyme B is expressed by cytotoxic lymphocytes and induces rapid target cell apoptosis. 


Catalog Number: (10229-210)
Supplier: Bioss
Description: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.


Catalog Number: (10461-994)
Supplier: Bioss
Description: Component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. Involved in apoptosis by acting as a death receptor-associated protein that mediates apoptosis. Also involved in glucose homeostasis in pancreatic islet. Functions as an adapter/mediator in replication stress-induced signaling that leads to the activation of CHEK1.


Catalog Number: (10328-170)
Supplier: Bioss
Description: The protein encoded by this gene is a member of the serine/threonine protein kinase family. This kinase was shown to be activated rapidly during Fas mediated apoptosis in Jurkat cells. In response to Fas receptor ligation, it phosphorylates TIA1, an apoptosis promoting nuclear RNA binding protein. The encoded protein is a strong inducer of lymphocyte apoptosis. Two transcript variants encoding different isoforms have been found for this gene. Other variants exist, but their full length natures have not yet been determined.


Catalog Number: (75934-614)
Supplier: Rockland Immunochemical
Description: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A human DNA fragmentation factor (DFF) was identified recently which is cleaved by caspase-3 during apoptosis. Mouse homologue of human DFF was identified as a DNase inhibitor designated ICAD, for inhibitor of caspase-activated DNase. Upon cleavage of DFF/ICAD, a caspase activated deoxyribonuclease (CAD) is released and activated and eventually causes the degradation of DNA in the nuclei. Therefore, the cleavage of CAD inhibitor molecule DFF/ICAD, which causes DNase activation and DNA degradation, is the hallmark of apoptotic cell death.


Catalog Number: (75931-000)
Supplier: Rockland Immunochemical
Description: Phosphoinositide 3 kinase enhancer (PIKE) is a recently identified nuclear GTPase that interacts with nuclear phosphoinositide 3-kinase (PI3 kinase) to stimulate its lipid kinase activity. PIKE exists in multiple isoforms; a shorter C-terminal isoform (PIKE-A) has also been identified as centaurin gamma 1. The longest isoform (PIKE-L) has been shown to bind to the adaptor protein Homer and thereby link to metabotropic glutamate receptors, leading to activation of PI3 kinase activity and prevention of neuronal apoptosis. Overexpression of PIKE-A enhances Akt activity and promotes cancer cell invasion, whereas decreased expression of PIKE-A via dominant negative expression of PIKE-A or PIKE-A knockdown inhibits these processes. In many human cancers, expression of PIKE-A is enhanced, leading to increased Akt activity and preventing apoptosis.


Catalog Number: (10229-214)
Supplier: Bioss
Description: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.


Catalog Number: (10229-218)
Supplier: Bioss
Description: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.


Supplier: Enzo Life Sciences
Description: A biologically active, cell-permeable, but nonphysiologic ceramide analog. It activates protein phosphatase 2A and MAP kinase (MAPK/ERK), suppresses insulin-induced tyrosine phosphorylation and inhibits glycoprotein traffic by the secretory pathway. It inhibits diacylglycerol accumulation and phospholipase D activation in fibroblasts. It induces an arrest at the G0/G1 transition of the cell cycle (10μM) and causes apoptosis (15μM or greater) in Molt-4 leukemia cells.

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