"Prosci"

Supplier: Prosci

ARTS Antibody: Apoptosis is related to many diseases and development. Mitochondrial proteins, such as cytochrome c, Apaf-1, and AIF play important role in apoptosis. A novel mitochondrial septin-like protein was identified recently and designated ARTS for apoptosis related protein in TGF-beta signaling pathway. ARTS that is encoded by the human septin H5/PNUTL2/CDCrel2b gene is located to mitochondria and translocates to the nucleus when apoptosis occurs. ARTS is expressed in many tissues. It enhances cell death induced by TGF-beta and, to a lesser extent, by other apoptotic agents, such as TNF-alpha and Fas ligand.

Supplier: Prosci

NALP2 Antibody: NALP2 belongs to a family of cytoplasmic proteins that have been implicated in cell responses to apoptotic and inflammatory stimuli. Unlike the prototypical NALP protein NALP1, NALP2 only contains a NACHT domain, leucine rich repeat (LRR), and pyrin-containing domain (PYD). This protein interacts with the adapter protein ASC in addition to CARD8 and caspase-1 to form an inflammasome with high proIL-1 beta -processing activity and is thought to function as a modulator of NF-kappa B and procaspase-1 activation in macrophages. It has also been suggested that NALP2, in addition to other NALP family members, can act as innate sensors of pathogens in a manner similar to the toll-like receptors (TLRs). At least two alternatively spliced transcript variants encoding distinct isoforms have been found for NALP2.

Supplier: Prosci

Bmf Antibody: Apoptosis is related to many diseases and development. Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain is a potent death domain. BH3-only proteins, including Bad, Bid, Bik, Hrk, Bim, Noxa, and PUMA, form a growing subclass of the Bcl-2 family. A novel BH3-only protein was recently identified in human and mouse and designated Bmf (for Bcl-2-modifing factor). The BH3 domain in Bmf is required both for binding to Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf associates with the dynein light chain 2 (DLC2) component of the myosin V motors and is sequestered by the cell's actin cytoskeleton. Disruption of the actin cytoskeleton, either by depolymerization of actin filaments or by detachment of cells from the extracellular matrix, triggers release and activation of Bmf, initiating the downstream apoptotic program. Bmf is constitutively expressed in many tissues.

Supplier: Prosci

Bmf Antibody: Apoptosis is related to many diseases and development. Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain is a potent death domain. BH3-only proteins, including Bad, Bid, Bik, Hrk, Bim, Noxa, and PUMA, form a growing subclass of the Bcl-2 family. A novel BH3-only protein was recently identified in human and mouse and designated Bmf (for Bcl-2-modifing factor). The BH3 domain in Bmf is required both for binding to Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf associates with the dynein light chain 2 (DLC2) component of the myosin V motors and is sequestered by the cell's actin cytoskeleton. Disruption of the actin cytoskeleton, either by depolymerization of actin filaments or by detachment of cells from the extracellular matrix, triggers release and activation of Bmf, initiating the downstream apoptotic program. Bmf is constitutively expressed in many tissues.

Supplier: Prosci

EndoG Antibody: The fragmentation of nuclear DNA is a hallmark of apoptotic cell death. The activities of caspase and nuclease are involved in the DNA fragmentation. Caspase-activated deoxyribonuclease (CAD), also termed DNA fragmentation factor (DFF40), is one such nuclease, and is capable of inducing DNA fragmentation and chromatin condensation after cleavage by caspase-3 of its inhibitor ICAD/DFF45. Caspase and CAD independent DNA fragmentation also exists. Recent studies demonstrated that another nuclease, endonuclease G (endoG), is specifically activated by apoptotic stimuli and is able to induce nucleosomal fragmentation of DNA independently of caspase and DFF/CAD. EndoG is a mitochondrion-specific nuclease that translocates to the nucleus and cleaves chromatin DNA during apoptosis. The homologue of mammalian EndoG is the first mitochondrial protein identified to be involved in apoptosis in C. elegans. EndooG also cleaves DNA in vitro.

Supplier: Prosci

NALP1 Antibody: NALP1 belongs to a family of cytoplasmic proteins that have been implicated in cell responses to apoptotic and inflammatory stimuli. It contains a caspase recruitment domain (CARD) in addition to a NACHT domain and leucine rich repeat (LRR). This protein interacts strongly with caspase 2 and weakly with caspase 9, as well as with Apaf-1. Transient overexpression of this gene in cultured cells was sufficient to induce apoptosis. NALP1 mRNA and protein expression levels in myeloid leukemia cells are increased following CREB (cAMP-response element binding protein) activation, suggesting that NALP1 may contribute to modulate the response of these cells to pro-inflammatory stimuli. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for NALP1.

Supplier: Prosci

AATF Antibody: AATF (apoptosis antagonizing transcription factor) was initially discovered as an interaction partner of ZIP kinase (ZIPK), a member of death-associated protein (DAP) kinase family of pro-apoptotic serine/threonine kinases. AATF is a phosphoprotein containing an acidic region and a putative leucine zipper domain and nuclear localization signal, features which are typical of transcription factors. AATF inhibits the ZIPK-mediated pro-apoptotic pathway and may activate other anti-apoptotic pathways. Recently, it has also been shown to protect neural cells against oxidative damage induced by amyloid b-peptide and to inhibit aberrant production of the beta-peptide by interacting with Par-4 (prostate apoptosis response-4), another pro-apoptotic leucine zipper protein that is associated with neuronal degeneration in Alzheimer's disease (AD), suggesting that AATF may have potential therapeutic applications in both familial and sporadic forms of AD.

Supplier: Prosci

PUMA Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 upregulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse. PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMA-alpha and PUMA-beta. PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.

Supplier: Prosci

PUMA Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 upregulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse. PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMA-alpha and PUMA-beta. PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.

Supplier: Prosci

p53DINP1 Antibody: Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible gene was identified recently and designated p53DINP1 (for p53-dependent damage-inducible nuclear protein 1) and SIP (for stress induced protein) in human and mouse. A p53DINP1 antisense oligonucleotide inhibits and overexpression of p53DINP1 enhances Ser46 phosphorylation of p53, induction of p53AIP1, and cell death induced by DNA double-strand breaks. p53DINP1 may regulate p53-dependent apoptosis through phosphorylation at Ser46 and induction of p53AIP1. The p53DINP1/SIP gene encodes two proteins of 27 and 18 kDa in human and mouse termed p53DINP1-alpha and p53DINP1-beta or SIP27 and SIP18. p53DINP1/SIP is expressed in many tissues and induced by a variety of stress agents including UV stress, mutagenic stress, heat shock, and oxidative stress.

Supplier: Prosci

OMI Antibody: 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: Prosci

TTC5 Antibody: Tetratricopeptide repeat protein 5 (TTC5) is a member of a diverse group of functionally distinct proteins that are characterized by containing one or more tetratricopeptide repeats. Each motif consists of two anti-parallel a-helices such that tandem arrays of TPR motifs generate a right-handed helical structure with an amphipathic channel that may serve to accommodate the complementary region of a target protein. While the exact function of TTC5 remains unclear, it is thought that the TPR motifs serve to mediate protein-protein interactions such as those seen with protein chaperones HSP70 and HSP90 and some proteins involved in cell stress response signaling pathways such as protein phosphatase 5, suggesting that TTC5 may also function via protein-protein interactions mediated by its TPR motifs.

Supplier: Prosci

DEDD2 Antibody: Apoptotic signals are often triggered by cell surface death receptors through protein-protein interactions mediated by conserved domains such as the death effector domain. A novel death effector domain (DED)-containing protein, DEDD2, has been recently identified and its over-expression in transfected cells induces moderate apoptosis and results in substantial sensitization to apoptosis induced by Fas, TRAIL, and FADD. More recently, work has shown that DEDD2 can bind caspase-8 and -10 in addition to FLIP but not FADD. Like the related protein DEDD, DEDD2 translocates from the cytosol to the nucleus upon induction of apoptosis, and it has been suggested that DEDD2 may target caspase-8 to the nucleus and that DEDD2 thus plays a critical role in death receptor-induced apoptosis. At least two alternatively spliced transcript variants encoding distinct isoforms have been found for DEDD2.

Supplier: Prosci

PAK6 Antibody: The p21-activated kinases (PAKs) are serine-threonine kinases that bind to the active forms of Cdc42 and Rac. They are divided into two groups, the first of which include PAK1, 2 and 3, and can be activated by Cdc42/Rac binding. Group 1 PAKs contain an autoinhibitory domain whose activity is regulated by Cdc42/Rac binding. The group 1 PAKs are known to be involved in cellular processes such as gene transcription, apoptosis, and cell morphology and motility. Much less is known about the second group, which includes PAK4, 5 and 6. These proteins are not activated by Cdc42/Rac binding. PAK6 was initially identified as an androgen receptor in a yeast two hybrid screen and was found to be highly expressed in testis and prostate tissues. Later experiments have shown it to be activated by MAP kinase kinase 6 and p38 MAP kinase, suggesting that PAK6 may play a role in the cellular response to stress-related signals.

Supplier: Prosci

PAK5 Antibody: The p21-activated kinases (PAKs) are serine-threonine kinases that bind to the active forms of Cdc42 and Rac. They are divided into two groups, the first of which include PAK1, 2 and 3, and can be activated by Cdc42/Rac binding. Group 1 PAKs contain an autoinhibitory domain whose activity is regulated by Cdc42/Rac binding. The group 1 PAKs are known to be involved in cellular processes such as gene transcription, apoptosis, and cell morphology and motility. Much less is known about the second group, which includes PAK4, 5 and 6. These proteins are not activated by Cdc42/Rac binding. PAK5 was initially identified as a kinase expressed primarily in brain that while possessing a kinase domain and GTPase binding domain similar to PAK4 and PAK6, is completely different from both. Expression of PAK5 in neural based cell lines resulted in neurite outgrowth suggesting that PAK5 may be involved in regulating the cytoskeletal changes necessary for promoting neurite outgrowth. Other experiments suggest that unlike the other PAKs, PAK5 may inhibit apoptosis by phosphorylating the Bcl-2 family member Bad.

Supplier: Prosci

PAK4 Antibody: The p21-activated kinases (PAKs) are serine-threonine kinases that bind to the active forms of Cdc42 and Rac. They are divided into two groups, the first of which include PAK1, 2 and 3, and can be activated by Cdc42/Rac binding. Group 1 PAKs contain an autoinhibitory domain whose activity is regulated by Cdc42/Rac binding. The group 1 PAKs are known to be involved in cellular processes such as gene transcription, apoptosis, and cell morphology and motility. Much less is known about the second group, which includes PAK4, 5 and 6. These proteins are not activated by Cdc42/Rac binding. PAK4 was initially identified as a novel effector of Cdc42Hs. Co-expression of PAK4 and Cdc42Hs resulted in induction of filopodia and actin polymerization, showing that it is involved in cytoskeletal reorganization. Other experiments have shown PAK4 to be essential for embryonic viability and proper neuronal development. PAK4 has also been implicated in anchorage-independent growth of tumor cells and is required for activation of several cancer prosurvival pathways.