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Catalog Number: (75790-850)
Supplier: Prosci
Description: Cytochrome C (CYCS) is a small heme protein that belongs to the cytochrome c family. It is found loosely associated with the inner membrane of the mitochondrion. Cytochrome C is a highly soluble protein that functions as a central component of the electron transport chain in mitochondria. CYCS transfers electrons between Complexes III (Coenzyme Q - Cyt C reductase) and IV (Cyt C oxidase). CYCS 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: (10748-612)
Supplier: Prosci
Description: XEDAR Antibody: X-linked ectodysplasin-A2 receptor (XEDAR) is a recently isolated member of the tumor necrosis factor receptor family that is highly expressed during embryonic development and binds to ectodysplatin-A2 (EDA-A2). Two predominantly expressed isoforms, XEDAR-s and XEDAR-L, differ by only a 21-amino region at the juxtamembrane region of the cytoplasmic domain. Neither isoform possesses a death domain and both have been shown to act mainly through TRAF3 and TRAF6 to activate the NF-kappa B and JNK pathways. Cells transfected with XEDAR and treated with EDA-A2 cause the assembly of a secondary complex containing FADD, caspase-8 and caspase-10, leading to the activation caspase-8 and caspase-3, and finally apoptosis. The EDA-A2-induced apoptosis is dependent on caspase-9 activation, as various pharmacological and genetic inhibitors of caspase-8 blocked apoptosis following EDA-A2 treatment.


Catalog Number: (10748-630)
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.


Catalog Number: (10801-050)
Supplier: Rockland Immunochemical
Description: Cyclin O, also known as CCNO, has recently been identified as a Cdk1- and Cdk2-activating cyclin specific to apoptosis in lymphoid cells. Cyclin O binds to and activates Cdk2 in response to instrinsic apoptotic stimuli such as glucocorticoids or DNA-damaging agents. Supression of Cyclin O expression by shRNA leads to the inhibition of glucocorticoid and DNA-damage-induced apoptosis due to a failure of apical caspase activation while leaving the CD95 death receptor-mediated apoptosis intact. Note: this gene, which had a previous symbol of UNG2, was erroneously identified as a uracil DNA glycosylase. A later publication identified this gene's product as a cyclin protein family member.


Catalog Number: (10334-416)
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: (76116-392)
Supplier: Bioss
Description: Receptor for TNFSF6/FASLG. 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. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (<i>in vitro</i>).


Catalog Number: (10800-344)
Supplier: Rockland Immunochemical
Description: 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.


Catalog Number: (76085-408)
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). Regulates UV radiation-induced DNA damage response mediated by CDKN1A.


Catalog Number: (75934-650)
Supplier: Rockland Immunochemical
Description: 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: (10231-976)
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: (10070-036)
Supplier: Prosci
Description: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Implicated in Notch signaling cross-over.


Catalog Number: (75908-762)
Supplier: Biotium
Description: MAb B-R18 specifically recognizes CD95, also known as Fas, a transmembrane glycoprotein with a MW of 40-45 kDa, containing 8 kDa of N-glycosidic-linked polysaccharide. It is a receptor for TNFSF6/FASLG, a member of the nerve growth factor receptor/tumor necrosis factor superfamily, mediating receptor-triggered apoptosis. 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. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro). CD95 antigen is expressed on the surface of various cell types, preferentially on the CD45RAlow CD45ROhigh subset of memory T lymphocytes.


Catalog Number: (10749-446)
Supplier: Prosci
Description: Noxa Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes including p53R2, p53AIP1, and PUMA. A new p53 target gene, Noxa, was recently identified, which encodes a protein belonging to the subfamily of BH3-only proapoptic proteins. Noxa and PUMA are both transcriptional targets of p53 and BH3-only proteins. X-ray irradiation increased p53-dependent Noxa mRNA and protein levels. Noxa, when ectopically expressed, interacted with anti-apoptotic Bcl-2 family members, resulting in the activation of caspase-9. Noxa, like PUMA, localized to mitochondria and induces apoptosis in response to p53. Noxa and PUMA may represent direct mediators of p53-induced apoptosis. Increased levels of p53 and its target gene Noxa was found in the impaired tumor development.


Catalog Number: (10801-048)
Supplier: Rockland Immunochemical
Description: Cyclin O, also known as CCNO, has recently been identified as a Cdk1- and Cdk2-activating cyclin specific to apoptosis in lymphoid cells. Cyclin O binds to and activates Cdk2 in response to instrinsic apoptotic stimuli such as glucocorticoids or DNA-damaging agents. Supression of Cyclin O expression by shRNA leads to the inhibition of glucocorticoid and DNA-damage-induced apoptosis due to a failure of apical caspase activation while leaving the CD95 death receptor-mediated apoptosis intact. Note: this gene, which had a previous symbol of UNG2, was erroneously identified as a uracil DNA glycosylase. A later publication identified this gene's product as a cyclin protein family member.


Catalog Number: (10231-906)
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: (89361-276)
Supplier: Genetex
Description: Apoptosis can be inhibited by a group of proteins called inhibitors of apoptosis (IAPs). These proteins contain a BIR (baculovirus IAP repeat) domain near the amino-terminus. The BIR domain can bind some caspases. Many members of the IAP family of proteins block proteolytic activation of caspase-3 and ~7. For example, XIAP, cIAP 1 and cIAP 2 appear to block cytochrome c-induced activation of caspase-9, thereby preventing initiation of the caspase cascade. Since cIAP 1 and cIAP 2 were first identified as components in the cytosolic death domain-induced complex associated with the TNF family of receptors, they may inhibit apoptosis by additional mechanisms.


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