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Catalog Number: (75843-258)
Supplier: BIOGEMS INTERNATIONAL INC.
Description: The RIK-2 monoclonal antibody recognizes human CD253, otherwise known as the TNF-related apoptosis inducing ligand (TRAIL) or tumor necrosis factor (ligand) superfamily member 10 (TNFSF10). TRAIL is a cytotoxic protein, which activates rapid apoptosis in tumor cells, but not in normal cells. TRAIL-induced apoptosis is achieved through binding to two death-signaling receptors, DR4 and DR5. These receptors belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain", which activates the cell's apoptotic machinery. The RIK-2 antibody is reported to block cellular apoptosis induced by TRAIL.


Catalog Number: (77439-280)
Supplier: Bioss
Description: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive.


Catalog Number: (10230-002)
Supplier: Bioss
Description: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.


Catalog Number: (10229-992)
Supplier: Bioss
Description: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.


Catalog Number: (10342-276)
Supplier: Bioss
Description: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity).


Catalog Number: (10342-254)
Supplier: Bioss
Description: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity).


Catalog Number: (10321-364)
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: (10351-640)
Supplier: Bioss
Description: FADD (Fas Associated Death Domain) is an apoptosis adapter molecule enabling transduction of the apoptosis signal initiated via the FasL/Fas receptor interaction. The protein contains a C terminal death domain that interacts with the Fas receptor death domain. The N terminus contains a death effectors domain (DED) which recruits caspase to the death inducing signaling complex (DISC) and initiates the apoptotic caspase cascade. Recruitment of Caspase 8 to the Fas receptor results in oligomerization of the Caspase 8 protein, which in turn drives its autoactivation through self-cleavage. Activated Caspase 8 then activates other downstream caspases including Caspase 9, thereby commiting the cell to undergo apoptosis. FADD is implicated in non-apoptotic cellular pathways such as the regulation of cell cycle machinery in T lymphocytes. This is connected to the phosphorylation state of FADD and to the FasL/TRAIL induced transcriptional activation of cfos protooncogene. FADD also interacts with the hepatitis C virus core protein in the HEK 293 cell line.


Catalog Number: (76080-012)
Supplier: Bioss
Description: Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Isoform 2 lacks activity is an dominant-negative inhibitor of caspase-9.


Catalog Number: (10321-362)
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: (10800-566)
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. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3. Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation. Caspase-9 is also activated by granzyme B and CPP32. Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNFa, TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues.


Catalog Number: (10800-050)
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. The mammalian homologues of the key cell death gene CED-4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease-activating factor 1). Apaf1 binds to cytochrome c (Apaf-2) and caspase-9 (Apaf-3), which leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Apaf1 can also associate with caspase-4 and caspase-8. Apaf1 is ubiquitously expressed in human tissues.


Catalog Number: (89415-250)
Supplier: Prosci
Description: ASK1 Antibody: Mitogen-activated protein (MAP) kinase cascades are activated in response to various extracellular stimuli, including cytokines, growth factors and environmental stresses. A novel MAP kinase kinase kinase (MAPKKK) was recently identified and designated ASK1 (for apoptosis signal-regulating kinase 1) and MAPKKK5. ASK1 activated two different subgroups of MAPKK, MKK4 and MKK6, which in turn activated c-Jun N-terminal kinase (JNK) and p38 MAP kinase, respectively. ASK1/MAPKKK5 is activated by TNFR and Fas through the interaction with members of the TRAF family and Fas-associated protein Daxx. Overexpression of ASK1 induced apoptotic cell death, and a catalytically inactive form of ASK1 inhibited TNF-alpha -induced apoptosis. ASK1 is expressed in variety of human and mouse tissues.


Catalog Number: (89360-154)
Supplier: Genetex
Description: Certain serine/threonine protein kinases, such as ASK1, RIP, DAP, and ZIP kinases, are mediators of apoptosis. Receptor interacting proteins including RIP and RIP2/RICK mediate apoptosis induced by TNFR1 and Fas, two prototype members in the death receptor family. A novel member in the RIP kinase family was recently identified and designated RIP3. RIP3 contains N-terminal kinase domain but, unlike RIP or RIP2, lacks the C-terminal death or CARD domain. RIP3 binds to RIP and TNFR1, mediates TNFR1 induced apoptosis, and attenuates RIP and TNFR1 induced NF-kB activation. Over expression of RIP3 induces apoptosis and NF-kB activation. The messenger RNA of RIP3 is expressed in a subset of adult tissues.


Catalog Number: (10328-320)
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: (77439-968)
Supplier: Bioss
Description: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin.


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