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Catalog Number: (89360-168)
Supplier: Genetex
Description: Members in the TNF superfamily regulate immune responses and induce apoptosis. A novel member in the TNF family was recently identified by several groups and designated BAFF (for B cell Activating Factor belonging to the TNF Family), BLyS (for B Lymphocyte Stimulator), TALL1 (for TNF- and ApoL- related Leukocyte-expressed Ligand), and THANK (for TNF Homologue that Activate Apoptosis, NFkB and c-jun N-terminal Kinase). BAFF/BLyS was characterized as a B cell stimulator since it induced B cell proliferation and immunoglobulin secretion. Two receptors for BAFF were recently identified and designated TACI and BCMA. BAFF and its receptors are involved in the development of systemic lupus erythaematosus and other B cell associated autoimmune diseases. Like TNFa and TRAIL,THANK was shown to activate NF-kB and c-jun N terminal kinase (JNK) and to induce apoptosis.


Catalog Number: (10229-196)
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: (10072-542)
Supplier: Prosci
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 to 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 soluble Fas 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: (10314-446)
Supplier: Bioss
Description: Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite (in vitro). Isoform 2: Has a role in spermiogenesis.


Catalog Number: (10334-408)
Supplier: Bioss
Description: Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional corepressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively.


Catalog Number: (89154-392)
Supplier: Enzo Life Sciences
Description: Caspase-11 not only activates caspase-1, that is required for the maturation of proinflammatory cytokines such as interleukin-1 (IL-1) and interleukin-18 (IL-18), but also activates caspase-3, leading to cellular apoptosis under pathological conditions. In most cells, caspase-11 is only expressed upon induction with pro-inflammatory stimuli. Caspase-11 is an essential mediator of endotoxic shock and caspase-11-deficient mice are resistant to endotoxic shock. LPS-induced caspase-11 regulates lymphocyte apoptosis by activating both caspase-3 and caspase-7. Human caspase-4, thought to be the homolog of mouse caspase-11, may be an effective therapeutic target for treatment of septic shock.


Catalog Number: (10454-130)
Supplier: Bioss
Description: DRAK1 (DAP kinase-related apoptosis-inducing protein kinase 1) is a novel member of the ser/thr protein kinase family, which mediate apoptosis through their catalytic activities. The full-length cDNA encodes a deduced 414-amino acid protein with a molecular mass of 46.56 kD. DRAKs contain an N-terminal kinase domain and a C-terminal regulation domain. DRAK1 messenger RNA appears to be ubiquitously expressed in human tissues. Overexpression of DRAK1 induces apoptosis. It has been shown in vitro that DRAK1 is capable of autophosphorylation and of phosphorylating the myosin light chain as an exogenous substrate, and that the noncatalytic C terminus is crucial for full kinase activity.


Catalog Number: (10325-830)
Supplier: Bioss
Description: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis (By similarity).


Catalog Number: (10454-346)
Supplier: Bioss
Description: DRAK1 (DAP kinase-related apoptosis-inducing protein kinase 1) is a novel member of the ser/thr protein kinase family, which mediate apoptosis through their catalytic activities. The full-length cDNA encodes a deduced 414-amino acid protein with a molecular mass of 46.56 kD. DRAKs contain an N-terminal kinase domain and a C-terminal regulation domain. DRAK1 messenger RNA appears to be ubiquitously expressed in human tissues. Overexpression of DRAK1 induces apoptosis. It has been shown in vitro that DRAK1 is capable of autophosphorylation and of phosphorylating the myosin light chain as an exogenous substrate, and that the noncatalytic C terminus is crucial for full kinase activity.


Catalog Number: (10350-556)
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: (10466-452)
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: (10750-416)
Supplier: Prosci
Description: PDCD5 Antibody: Programmed cell death 5 (PDCD5), a human apoptosis-related protein, is thought to play an early and universal role in apoptosis. PDCD5 is widely expressed and is upregulated in cells undergoing apoptosis, where it translocates rapidly from the cytoplasm to the nucleus. PDCD5 has a compact core structure of low flexibility with two mobile alpha-helices at N-terminal and a flexible unstructured C-terminal region. The charged residues are crucial for the ability of apoptosis-promoting and cell translocation of the protein. PDCD5 can facilitate apoptosis and enhance TAJ/TROY-induced paraptosis-like cell death. PDCD5 may play a dual role in the Tip60 pathway. It interacts with Tip60 and functions as a Tip60 co-activator to promote apoptosis. The nucleotide polymorphisms in the 5'-upstream region of PDCD5 affect promoter activity and the susceptibility of a Chinese population to develop chronic myelogenous leukemia and may represent a novel tumor suppressor gene influencing lung cancer.


Catalog Number: (89351-532)
Supplier: Genetex
Description: Bcl-2 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). [Provided by RefSeq]


Catalog Number: (10751-886)
Supplier: Prosci
Description: IL-15 Antibody: Interleukin 15 (IL-15) is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and IL-2 share many biological activities as both have been found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between IL-15 and IL-2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. In mouse, studies suggest that IL-15 may increase the expression of apoptosis inhibitor Bcl-xL, possibly through the transcription activation activity of STAT6, and thus prevent apoptosis.


Catalog Number: (10062-526)
Supplier: Prosci
Description: IL-15 Antibody: Interleukin 15 (IL-15) is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and IL-2 share many biological activities as both have been found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between IL-15 and IL-2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. In mouse, studies suggest that IL-15 may increase the expression of apoptosis inhibitor Bcl-xL, possibly through the transcription activation activity of STAT6, and thus prevent apoptosis.


Catalog Number: (89416-082)
Supplier: Prosci
Description: Bfl-1 Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells and is caused by caspase activation. Proteins that comprise the Bcl-2 family appear to control the activation of these enzymes. One such member is multi-domain antiapoptotic protein Bfl-1, which is overexpressed in stomach and other cancers. Bfl-1 can interact with Bax and suppress apoptosis by inhibiting the release of cytochrome c and caspase-3 activation. It is upregulated in cisplatin-resistant human bladder tumors, suggesting that its expression may be important for cisplatin resistance and inhibition of apoptosis in cancer cells. At least two isoforms of Bfl-1 are known to exist.


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