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anti-Mouse (Murine) DIABLO Anticorps:
anti-Human DIABLO Anticorps:
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Human Polyclonal DIABLO Primary Antibody pour ICC, IF - ABIN252299
Yoo, Kim, Kim, Park, Park, Jeon, Jung, Lee, Lee: Immunohistochemical analysis of Smac/DIABLO expression in human carcinomas and sarcomas. dans APMIS : acta pathologica, microbiologica, et immunologica Scandinavica 2003
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Human Monoclonal DIABLO Primary Antibody pour ICC, IF - ABIN153019
Wang, Zhu, Drozda, Zhang, Stavrovskaya, Cattaneo, Ferrante, Kristal, Friedlander: Minocycline inhibits caspase-independent and -dependent mitochondrial cell death pathways in models of Huntington's disease. dans Proceedings of the National Academy of Sciences of the United States of America 2003
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Mouse (Murine) Monoclonal DIABLO Primary Antibody pour ELISA, FACS - ABIN4354647
Tikoo, OReilly, Day, Verhagen, Pakusch, Vaux: Tissue distribution of Diablo/Smac revealed by monoclonal antibodies. dans Cell death and differentiation 2002
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Polyclonal DIABLO Primary Antibody pour IP, ELISA - ABIN539482
Wu, Chai, Suber, Wu, Du, Wang, Shi: Structural basis of IAP recognition by Smac/DIABLO. dans Nature 2001
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Human Polyclonal DIABLO Primary Antibody pour IHC (p), WB - ABIN541409
Du, Fang, Li, Li, Wang: Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. dans Cell 2000
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Human Polyclonal DIABLO Primary Antibody pour IHC (p), WB - ABIN541411
Srinivasula, Datta, Fan, Fernandes-Alnemri, Huang, Alnemri: Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway. dans The Journal of biological chemistry 2000
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Human Polyclonal DIABLO Primary Antibody pour IHC, WB - ABIN223042
Haudek, Taffet, Schneider, Mann: TNF provokes cardiomyocyte apoptosis and cardiac remodeling through activation of multiple cell death pathways. dans The Journal of clinical investigation 2007
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Human Polyclonal DIABLO Primary Antibody pour WB - ABIN540294
Sakabe, Ikeda, Nakatani, Kawada, Imanaka-Yoshida, Yoshida, Yamagishi, Nakajima: Rho kinases regulate endothelial invasion and migration during valvuloseptal endocardial cushion tissue formation. dans Developmental dynamics : an official publication of the American Association of Anatomists 2005
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Human Polyclonal DIABLO Primary Antibody pour IHC (p), ELISA - ABIN3044515
You, Li, Jin, Zheng, Chen, Yang: Genistein protects against Aβ25-35 induced apoptosis of PC12 cells through JNK signaling and modulation of Bcl-2 family messengers. dans BMC neuroscience 2017
Human Polyclonal DIABLO Primary Antibody pour WB - ABIN537990
Kim, Eom, Cheong, Choi, Lee, Yang, Min: Protein kinase CK2alpha as an unfavorable prognostic marker and novel therapeutic target in acute myeloid leukemia. dans Clinical cancer research : an official journal of the American Association for Cancer Research 2007
We report that an Smac-mimetic selectively induces TNF-alpha-dependent cystic renal epithelial cell death, leading to the removal of cystic epithelial cells from renal tissues and delaying cyst formation.
Results demonstrate an essential and apoptosis-independent function of SMAC in tumor suppression and provide new insights into the biology and targeting of colon cancer.
Identification of a novel anti-apoptotic E3 ubiquitin ligase that ubiquitinates antagonists of inhibitor of apoptosis proteins SMAC, HtrA2, and ARTS.
Loss of Smac/DIABLO alters both caspase-dependent and caspase-independent intrinsic programmed cell death.
Membrane-associated XIAP induces mitochondrial outer membrane permeabilization leading to cytochrome c and Smac release, which is dependent on Bax and Bak.
data suggest the existence of a redundant molecule or molecules capable of compensating for a loss of Smac/DIABLO function.
mitochondrial activation by Bid is required for reversing the inhibitor-of-apoptosis proteins inhibition through Smac release
Diablo was present within the mitochondria of healthy cells, but released into the cytosol following the induction of apoptosis by UV.
Transient focal ischemia was produced for 1 hour in mice. Mitochondrial levels of DIABLO increased after 2-11 h reperfusion. DIABLO increased in the cytosol after 5 h reperfusion, implying the translocation of DIABLO into the cytosol.
Bax and Bak differentially regulate the release of cytochrome c and Smac/DIABLO from mitochondria, and Smac/DIABLO can be used to sensitize cells that are deficient in Bax and Bak genes, or resistant to TRAIL.
Regulation of Smac/Diablo mRNA and protein expression is a mechanism by which lethal stimuli amplify their lethal potential in renal cells.
These results suggest that interaction among XIAP, Smac/DIABLO, and caspase-9 plays an important role in the regulation of apoptotic neuronal cell death after transient focal cerebral ischemia.
Smac/DIABLO is involved in the fragmentation and apoptosis of preimplantation embryos.
release of Smac/DIABLO from mitochondria to cytoplasm and the subsequent activation of caspase-9 and caspase-3 play important roles in H(2)O(2)-induced apoptosis in C2C12 myogenic cells
Smac/DIABLO and Hsp-70 proteins were upregulated 2-fold and 1.5-3-fold, respectively, after birth.
In response to autocrine TNFalpha signaling, the Smac mimetic promotes formation of a RIPK1-dependent caspase-8-activating complex, leading to apoptosis
TAK1, receptor-interacting kinase 1 (RIPK1) as well as canonical and non-canonical NF-kappaB signaling are differentially involved in Smac-induced cell death in breast cancer cells.
SMAC/Diablo possesses additional non-apoptotic functions related to regulating lipid synthesis essential for cancer growth and development and that this may explain SMAC/Diablo overexpression in cancer.
Positive expression for CD56 and CD11b with Low Smac/DIABLO Expression is associated with Chemoresistance in Acute Myeloid Leukaemia.
Mechanistic studies showed that Smac can inhibit the expression of Survivin, promote cell apoptosis of drug-resistant ovarian cancer cells and reverse the drug resistance.
Serum Smac expression level was significantly lower in the EAOC group than in the control group and benign ovarian tumor group (P< 0.05), while HE4 and CA125 expression levels were significantly higher in the EAOC group than the other two groups.
SMAC expression in locally advanced breast cancer is a novel favourable prognostic factor in LABC for pathological complete remission and disease-free survival.
administration of SMAC or BH3 mimetics following short-term paclitaxel treatment could be an effective therapeutic strategy for TNBC, while only BH3-mimetics could effectively overcome long-term paclitaxel resistance.
Antagonism strategies to modulate the actions of XIAP, cIAP1/2 and survivin are the central focus of current research and this review highlights advances within this field with particular emphasis upon the development and specificity of second mitochondria-derived activator of caspase (SMAC) mimetics (synthetic analogs of endogenously expressed inhibitors of IAPs SMAC/DIABLO).
analysis of Smac-mediated apoptosis in chronic lymphocytic leukemia cells
Data show that oncolytic viruses (OV) and second mitochondrial activator of caspase (Smac)-mimetic compounds (SMC) synergistically kill cancer cells directly.
Expressions of SDF-1, survivin and smac were significantly higher in epithelial ovarian cancer tissue than those in normal tissue.
Results indicate that Smac plays an important role in reticulum stress-induced apoptosis in human lens epithelial cells, suggesting its close association with cataract development.
Smac mimetic APG-1387 exerts a potent antitumor effect on nasopharyngeal carcinoma cells by inducing apoptosis.
These results reveal a pro-apoptotic function of PARL and identify PARL-mediated Smac processing and cytochrome c release facilitated by OPA1-dependent cristae remodelling as two independent pro-apoptotic pathways in mitochondria.
Study found a negative correlation between Smac and XIAP at the level of protein but not mRNA in non-small cell lung carcinoma (NSCLC) patients. Overexpressed XIAP could degrade through ubiquitination, the mature Smac inhibiting NSCLC apoptosis.
Report role of RIP1 in Smac mimetic mediated chemosensitization of neuroblastoma cells.
This review discusses the promise as well as some challenges at the translational interface of exploiting Smac mimetics as cancer therapeutics.
Data indicate that Smac/DIABLO showed an inverse correlation with inhibitor of apoptosis proteins XIAP, cIAP-1 and cIAP-2.
Data show that mitochondrial X-linked inhibitor of apoptosis protein (XIAP) entry requires apoptosis regulatory proteins Bax or Bak through mitochondrial permeabilization and Smac/DIABLO protein degradation.
SapC-DOPS acts through a mitochondria-mediated pathway accompanied by an early release of Smac and Bax.
hyperosmotic shock induces rapid calpain activation and high levels of Smac/DIABLO release from the mitochondria before significant amounts of cytochrome c are released to promote caspase-3 activation
Identification of the third vertebrate homologue of Smac/DIABLO.
This gene encodes an inhibitor of apoptosis protein (IAP)-binding protein. The encoded mitochondrial protein enters the cytosol when cells undergo apoptosis, and it moderates the caspase inhibition of IAPs. Multiple polyadenylation sites have been found for this gene. Four alternatively spliced transcript variants have been described for this gene, with two of them encoding different isoforms and the other two probably not encoding a protein.
Direct IAP-binding protein with low pI
, diablo homolog, mitochondrial
, second mitochondria-derived activator of caspase
, direct IAP binding protein with low PI
, direct IAP-binding protein with low pI
, diablo homolog
, mitochondrial diablo-like protein
, mitochondrial diablo
, second mitochondrial derived activator of caspases
, Second mitochondria-derived activator of caspase