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Catalog Number: (10232-006)
Supplier: Bioss
Description: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.


Catalog Number: (75930-628)
Supplier: Rockland Immunochemical
Description: Inhibitor of apoptosis proteins (IAPs) were initially identified in baculoviruses as proteins that inhibit apoptosis of the host cells to allow time for viral replication. Cellular homologues containing at least one baculoviral IAP repeat (BIR) motif essential for their anti-apoptosis activity have been identified in yeasts and higher organisms and often act by binding and inhibiting processed caspases. The activity of these proteins can be modulated by the expression of proteins such as Smac/DIABLO and XAF-1 which displace or prevent the binding of caspases by IAPs. Recently, a mitochondrial serine protease termed Omi/HtrA2 has been found to bind IAPs. Similar to Smac, Omi possesses a conserved IAP-binding motif, but acts to cleave IAPs to irreversibly inactivate IAPs and promote apoptosis.


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: (76196-048)
Supplier: Prosci
Description: Als2Cr2, also called STE20-related kinase adapter protein beta (STRAD beta) and ILPIP, is a serine/threonine protein kinase encoded by the STRADB gene, discovered as an XIAP interacting protein. It is a mediator of the XIAP/TAK1 activation of the JNK1 pathway, an apoptosis inhibition mechanism independent of XIAP inhibition of caspases. Alone, it only moderately activates JNKs, but its interaction with XIAP/TAK1 induces a much stronger activation of JNK1, protecting against Caspase 1- or Fas-induced apoptosis.


Catalog Number: (77437-550)
Supplier: Bioss
Description: Promotes caspase-mediated apoptosis. This proapoptotic activity is mediated predominantly through the activation of caspase-9. May be a component of the inflammasome, a protein complex which also includes NALP2, CARD8 and CASP1 and whose function would be the activation of proinflammatory caspases.


Catalog Number: (10813-944)
Supplier: Prosci
Description: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.


Catalog Number: (89415-384)
Supplier: Prosci
Description: Survivin Antibody: Apoptosis, or programmed cell death, is related to many diseases, such as cancer. Apoptosis is triggered by a variety of stimuli including members in the TNF family and prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. A novel IAP protein was recently identified and designated survivin, apoptosis inhibitor 4 (API4), and TIAP. Survivin/TIAP interacted with the processed form of caspase-3 and inhibited its proteolytic activity. Survivin/TIAP is predominantly expressed in tissues of embryos, transformed cell lines, and many human cancers and lymphomas.


Catalog Number: (10465-864)
Supplier: Bioss
Description: The death domain (DD) containing protein PIDD is a p53 target gene in an erythroleukemia cell line that undergoes G1 phase arrest and subsequent apoptosis after p53 expression. Independently, PIDD was also described as a DD-containing protein with unknown function. The N-terminal region of PIDD contains seven leucine-rich repeats (LRRs), a protein interaction motif found in various proteins with diverse functions, followed by two ZU-5 domains and a C-terminal DD. PIDD forms a complex with caspase-2 and the adaptor protein RAIDD. Increased PIDD expression results in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli, via interaction with caspase-2 and CRADD/RAIDD. PIDD also promotes apoptosis downstream of p53 as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. PIDD has also been shown to interact with NEMO/IKBKG and RIP1 and enhance sumoylation and ubiquitination of NEMO/IKBKG, an important component for activation of the transcription factor NF-kappa-B.


Catalog Number: (10350-554)
Supplier: Bioss
Description: 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).


Catalog Number: (10466-548)
Supplier: Bioss
Description: Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene but the biological validity of these variants has not been determined. [provided by RefSeq, Jul 2008].


Catalog Number: (10237-228)
Supplier: Bioss
Description: P19ARF Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development.


Catalog Number: (10780-646)
Supplier: Peprotech
Description: Fas Ligand (FasL) is a member of the TNF superfamily that is expressed on the cell surface of activated T cells. Binding of FasL to Fas Receptor triggers apoptosis in Fas-bearing cells. FasL has the ability to kill T cells and activated B cells, which leads to down-regulation of the immune response. The mechanism of Fas-induced apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. Both human and murine sFasL are fully active on human and murine cells. Recombinant Human sFas Ligand is a 17.9 kDa protein comprising the TNF-homologous region of FasL and contains an 8-residue N-terminal His-Tag.


Catalog Number: (10362-724)
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: (10231-314)
Supplier: Bioss
Description: Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity.


Catalog Number: (10797-302)
Supplier: Prosci
Description: Diablo homolog, mitochondrial (DIABLO) is also known as direct IAP-binding protein with low pI and second mitochondria-derived activator of caspase (SMAC), which can interact with BIRC2/c-IAP1, BIRC3/c-IAP2, XIAP/BIRC4, BIRC6/bruce and BIRC7/livin. Acting by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP),DIABLO can also promote apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Also, DIABLO inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Furthermore, DIABLO is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.


Catalog Number: (10239-752)
Supplier: Bioss
Description: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1.


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