Bcl-2 (phospho Ser70) antibody (B-cell CLL/lymphoma 2) for WB. Anti-Bcl-2 (phospho Ser70) pAb (GTX129653) is tested in Human samples. 100% Ab-Assurance.
Bcl-2 antibody [GT11210] (B-cell CLL/lymphoma 2) for WB. Anti-Bcl-2 mAb (GTX628905) is tested in Human samples. 100% Ab-Assurance.
We have identified a new pro-apoptotic Bcl-2-related protein Bok, based on its binding to an ovarian anti-apoptosis protein Mcl-1. In addition to its restricted expression in several reproductive tissues, Bok also shows a selective heterodimerization property by interacting with some (Mcl-1, BHRF1, and Bfl-1) but not other (Bcl-2, Bcl-xL, and Bcl-w) anti-apoptotic proteins. Coupled with findings showing that Bok-induced apoptosis could only be antagonized by selective anti-apoptotic proteins, the present data suggest that different pro- and anti-apoptotic Bcl-2 protein pairs may play tissue-specific roles in the regulation of apoptosis. Because of the restricted expression of Bok to ovarian granulosa cells and several reproductive tissues characterized by hormonally regulated cyclic cell turnover, further analyses of Bok action in the gonads and uterus could provide unique models to study the hormonal regulation of apoptosis. Because most of the Bcl-2-related proteins have been identified in the ...
The effect of Bcl-xL upon the developmental death of T cells was assessed by generating transgenic mice that expressed Bcl-xL within all thymocyte subsets. Bcl-xL protected thymocytes from a variety of apoptotic stimuli, including gamma irradiation, glucocorticoids, and anti-CD3 treatment. Bcl-xL altered thymocyte maturation, resulting in increased numbers of CD3int/hi and CD4-8+ thymocytes. Overall, the phenotype of Bcl-xL transgenics was essentially indistinguishable from a Bcl-2 transgenic model. Overexpression of Bcl-xL or Bcl-2 resulted in the down-regulation of the other molecule, providing further evidence of their reciprocal regulation. In a genetic test of redundancy, the Bcl-xL transgene rescued mature T cells in Bcl-2 null mice. Immunoprecipitation indicated that Bcl-xL, like Bcl-2, heterodimerized with the death-promoting molecule Bax in thymocytes. This in vivo model argues that Bcl-xL, like Bcl-2, functions in a common pathway to repress cell death. ...
Microtubule inhibiting agents (MIAs) characteristically induce phosphorylation of the major anti-apoptotic Bcl-2 family members Mcl-1, Bcl-2 and Bcl-xL, and while this leads to Mcl-1 degradation, the role of Bcl-2/Bcl-xL phosphorylation in mitotic death has remained controversial. We used siRNA knockdown of the anaphase-promoting complex activator, Cdc20, as a defined molecular system to investigate the role, specifically in mitotic death, of individual anti- apoptotic Bcl-2 proteins and their phosphorylated forms. We show that Cdc20 knockdown in HeLa cells induces mitotic arrest and subsequent mitotic death. Knockdown of Cdc20 in HeLa cells stably overexpressing untagged wild-type Bcl-2, Bcl-xL or Mcl-1 promoted phosphorylation of the overexpressed proteins in parallel with their endogenous counterparts. Overexpression of Bcl-2 or Bcl-xL blocked mitotic death induced by Cdc20 knockdown, phospho-defective mutants were more protective than wild-type proteins, and phospho-mimic Bcl-xL was unable ...
【Promotion】Abbkine Selected Primary Antibody-Click for Promotion details. Bcl-2 gene (B-cell lymphoma-2) is a member of Bcl-2 family, which is the earliest discovered apoptosis protein. It is an anti-apoptosis protei,,
Model for the inactivation of prosurvival Bcl-2-like proteins by the BH3-only proteins. It is proposed that prosurvival family members, like Bcl-w, normally b
Bcl-2-like 8, 0.1 mg. Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX.
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2000) AtBI-1, a plant homologue of Bax Inhibitor-1, suppresses Bax-induced cell death in yeast and is rapidly upregulated during wounding and pathogen challenge. The Plant Journal, 21 (4). pp. 393-399 ...
DNA double-strand breaks (DSBs) are mainly repaired either by homologous recombination (HR) or by nonhomologous end-joining (NHEJ) pathways. Here, we showed that myeloid cell leukemia sequence 1 (Mcl-1) acts as a functional switch in selecting between HR and NHEJ pathways. Mcl-1 was cell cycle-regulated during HR, with its expression peaking in S/G2 phase. While endogenous Mcl-1 depletion reduced HR and enhanced NHEJ, Mcl-1 overexpression resulted in a net increase in HR over NHEJ. Mcl-1 directly interacted with the dimeric Ku protein complex via its Bcl-2 homology 1 and 3 (BH1 and BH3) domains, which are required for Mcl-1 to inhibit Ku-mediated NHEJ. Mcl-1 also promoted DNA resection mediated by the Mre11 complex and HR-dependent DSB repair. Using the Mcl-1 BH1 domain as a docking site, we identified a small molecule, MI-223, that directly bound to BH1 and blocked Mcl-1-stimulated HR DNA repair, leading to sensitization of cancer cells to hydroxyurea- or olaparib-induced DNA replication ...
Title: Bcl-2 Proteins: Targets and Tools for Chemosensitisation of Tumor Cells. VOLUME: 3 ISSUE: 4. Author(s):Ali Bettaieb, Laurence Dubrez-Daloz, Sophie Launay, Stephanie Plenchette, Cedric Rebe, Severine Cathelin and Eric Solary. Affiliation:INSERM U517, IFR 100, 7 boulevard Jeanne dArc, 21000 Dijon, France.. Keywords:apoptosis, cell death, bcl-2, bh3-only proteins, mitochondria, antisense oligonucleotides, bh3 mimetics. Abstract: Proteins of the Bcl-2 family share one or several Bcl-2 homology (BH) regions and behave as pro- or antiapoptotic proteins. Prosurvival members such as Bcl-2 and Bcl-XL are supposed to preserve mitochondrial outer membrane integrity, thus preventing the release of soluble apoptogenic molecules. Pro-apoptotic members include BH3- only proteins that act as sensors of cellular damage and initiate the death process and Bax-like proteins that act downstream of BH3-only proteins to permeabilise the mitochondrial outer membrane. Whether BH3-only proteins directly activate ...
Research over the years has expanded the list of proteins structurally or functionally linked to BCL-2 (B-cell lymphoma-2), the product of a proto-oncogene identified almost thirty years ago. Discovery of the BCL-2 gene defined a new class of proto-oncogenes that block cell death without enhancing cell proliferation. Today, this protein group is formed by a family of BCL-2 homologs (which have phylogenetic relationships), and by a collection of evolutionarily and structurally unrelated proteins characterized by the presence of a region of local sequence similarity with BCL-2, termed the BH3 motif. BCL-2 homologous proteins share a similar α-helical bundle fold (the BCL-2 domain), have up to four different BH motifs (BH1-BH4), and can be either anti-apoptotic (e.g., BCL-2 and BCL-xL) or pro-apoptotic (e.g., BAX, BAK and BID). All the other (non-BCL-2 homologous) proteins possessing a functional BH3 motif are pro-apoptotic (such as the BH3-only member BIM or the BH3 motif-containing protein ...
Research over the years has expanded the list of proteins structurally or functionally linked to BCL-2 (B-cell lymphoma-2), the product of a proto-oncogene identified almost thirty years ago. Discovery of the BCL-2 gene defined a new class of proto-oncogenes that block cell death without enhancing cell proliferation. Today, this protein group is formed by a family of BCL-2 homologs (which have phylogenetic relationships), and by a collection of evolutionarily and structurally unrelated proteins characterized by the presence of a region of local sequence similarity with BCL-2, termed the BH3 motif. BCL-2 homologous proteins share a similar α-helical bundle fold (the BCL-2 domain), have up to four different BH motifs (BH1-BH4), and can be either anti-apoptotic (e.g., BCL-2 and BCL-xL) or pro-apoptotic (e.g., BAX, BAK and BID). All the other (non-BCL-2 homologous) proteins possessing a functional BH3 motif are pro-apoptotic (such as the BH3-only member BIM or the BH3 motif-containing protein ...
Lyoniresinol 3α-O-β-D-Glucopyranoside-Mediated Hypoglycaemia and Its Influence on Apoptosis-Regulatory Protein Expression in the Injured Kidneys of Streptozotocin-Induced Mice. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
DUBLIN, July 9, 2019 /PRNewswire/ -- The "Venclexta" report has been added to ResearchAndMarkets.coms offering. Drug Overview. Venclexta (venetoclax; AbbVie/Roche) is an inhibitor of the B-cell lymphoma-2 (BCL-2) family of proteins. This family of proteins is responsible for the regulation of cell death by either inducing or inhibiting apoptosis. Increased expression of BCL-2 can lead to resistance to apoptosis in cancer cells. Venclexta blocks the function of the BCL-2 protein, leading to an increase in pro-apoptotic proteins and restoration of normal apoptosis regulation ...
Tissue destruction that occurs upon infection with the bacterium Escherichia coli 0157:H17 is attributed in part to the bacterial factor verotoxin II (VTII), but the molecular mechanism of cell-death induction has not been clear. Suzuki et al. report that VTII has a pentameric sequence that is identical to a sequence found in the BH1 domain of mitochondrial Bcl-2, a protein that inhibits apoptosis. The BH1 domain of Bcl-2 mediates interaction with other Bcl-2 family members to suppress cell death. Biochemical analysis indicates that the pentameric sequence of VTII interacts with Bcl-2. When cells expressing Bcl-2 were treated with VTII, caspase 3 activation and subsequent apoptosis occurred. VTII also localized to mitochondria where Bcl-2 resides. The authors propose that VTII-Bcl-2 interaction is one of the death-induction mechanisms utilized by this bacterium. However, the molecular mechanism by which VTII induces cell death through Bcl-2 remains to be determined, but may involve blocking of ...
Venetoclax, also known as ABT-199 or GDC0199, is an orally bioavailable, selective small molecule inhibitor of the anti-apoptotic protein Bcl-2, with potential antineoplastic activity. Venetoclax mimics BH3-only proteins, the native ligands of Bcl-2 and apoptosis activators, by binding to the hydrophobic groove of Bcl-2 proteins thereby repressing Bcl-2 activity and restoring apoptotic processes in tumor cells.
The BH3-only apoptosis agonists BAD and NOXA target BCL-2 and MCL-1 respectively and co-operate to induce apoptosis. On this basis, therapeutic drugs targeting BCL-2 and MCL-1 might have enhanced activity if used in combination. We identified anti-leukaemic drugs sensitising to BCL-2 antagonism and drugs sensitising to MCL-1 antagonism using the technique of dynamic BH3 profiling, whereby cells were primed with drugs to discover whether this would elicit mitochondrial outer membrane permeabilisation in response to BCL-2-targeting BAD-BH3 peptide or MCL-1-targeting MS1-BH3 peptide. We found that a broad range of anti-leukaemic agents-notably MCL-1 inhibitors, DNA damaging agents and FLT3 inhibitors-sensitise leukaemia cells to BAD-BH3. We further analysed the BCL-2 inhibitors ABT-199 and JQ1, the MCL-1 inhibitors pladienolide B and torin1, the FLT3 inhibitor AC220 and the DNA double-strand break inducer etoposide to correlate priming responses with co-operative induction of apoptosis. ABT-199 in ...
Complete information for BAX gene (Protein Coding), BCL2 Associated X, Apoptosis Regulator, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Key Points. Novel BET inhibitors PLX51107 and PLX2853 induce apoptosis via induction of the proapoptotic BH3-only protein BIM.PLX51107 and PLX2853 are synergis
Sigma-Aldrich offers abstracts and full-text articles by [Haiqin Wu, Huqing Wang, Wenting Zhang, Xuanhui Wei, Jiaxin Zhao, Pu Yan, Chao Liu].
Apoptosis is initiated when Bcl-2 and its prosurvival relatives are engaged by proapoptotic BH3-only proteins via interaction of its BH3 domain with a groove on the Bcl-2-like proteins ...
In vivo resistance to first-line chemotherapy, including to glucocorticoids, is a strong predictor of poor outcome in children with acute lymphoblastic leukemia (ALL). Modulation of cell death regulators represents an attractive strategy for subverting such drug resistance. Here we report complete resensitization of multidrug-resistant childhood ALL cells to glucocorticoids and other cytotoxic agents with subcytotoxic concentrations of obatoclax, a putative antagonist of BCL-2 family members. The reversal of glucocorticoid resistance occurred through rapid activation of autophagy-dependent necroptosis, which bypassed the block in mitochondrial apoptosis. This effect was associated with dissociation of the autophagy inducer beclin-1 from the antiapoptotic BCL-2 family member myeloid cell leukemia sequence 1 (MCL-1) and with a marked decrease in mammalian target of rapamycin (mTOR) activity. Consistent with a protective role for mTOR in glucocorticoid resistance in childhood ALL, combination of ...
Most studies looking at the expression of Bcl-2 in cholangiocarcinoma report varying amounts of Bcl-2 protein expression in this disease.24 In contrast, a study looking at Bcl-2 protein expression in cholangiocarcinoma recently reported that none of the cholangiocarcinoma samples examined expressed the Bcl-2 protein.36 With Bcl-2 expression detected in the internal positive controls and in regenerating intrahepatic ductular epithelium, an observation reported previously,37 our inability to detect the of Bcl-2 protein is unlikely to be a result of poor antigen retrieval or low Bcl-2 antibody activity. There have been suggestions that in some cell types a reciprocal expression of survival proteins Bcl-2 and Bcl-XL occurs. Considering there are still many unanswered questions about the cellular control and preference of expression of the different Bcl-2 genes, this might explain the differences in reported findings. It may be that as we learn more about these proteins, reasons for the differences ...
Albany, New York, Dec 1, 2017: Apoptosis Regulator BAX (Bcl 2 Like Protein 4 or BCL2L4 or BAX) - Apoptosis regulator BAX or bcl-2-like protein 4 is a protein is encoded by the BAX gene. It accelerates programmed cell death by antagonizing the apoptosis repressor BCL2. It promotes activation of CASP3, and thereby apoptosis. It undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis under stress conditions.. Request For Free Sample - https://www.marketresearchhub.com/enquiry.php?type=S&repid=1389111. Apoptosis Regulator BAX (Bcl 2 Like Protein 4 or BCL2L4 or BAX) pipeline Target constitutes close to 7 molecules. Out of which approximately 3 molecules are developed by companies and remaining by the universities/institutes. The molecules developed by companies in Phase III, Phase II and Preclinical stages are 1, 1 and 1 respectively. Similarly, the universities portfolio in Preclinical and Discovery ...
Among the many target genes of the transcription factor NF-kappaB are p53 and c-myc, both of which are involved in apoptosis. This prompted us to investigate the role of NF-kappaB in this process. We report that NF-kappaB is potently activated upon serum starvation, a condition leading to apoptosis in 293 cells. Similar to Bcl-2, a transdominant-negative mutant of the NF-kappaB p65 subunit partially inhibited apoptosis, indicating a direct involvement of the transcription factor in induction of cell death. As expected, the p65 mutant suppresses kappaB-dependent gene expression. Surprisingly, transiently or stably overexpressed Bcl-2 had the same effect. The transcription inhibitory activity of the two proteins correlated with their cell death protective potential. Like Bcl-2, the related protein Bcl-xL but not Bcl-xS was able to suppress kB-dependent transcription. Bcl-2 inhibited NF-kappaB activity by an unusual mechanism. It did not prevent the release of IkappaB in the cytoplasm but ...
The BH3-mimetic ABT-737 and an orally bioavailable compound of the same class, navitoclax (ABT-263), have shown promising antitumor efficacy in preclinical and early clinical studies. Although both drugs avidly bind Bcl-2, Bcl-xL, and Bcl-w in vitro, we find that Bcl-2 is the critical target in vivo, suggesting that patients with tumors overexpressing Bcl-2 will probably benefit. In human non-Hodgkin lymphomas, high expression of Bcl-2 but not Bcl-xL predicted sensitivity to ABT-263. Moreover, we show that increasing Bcl-2 sensitized normal and transformed lymphoid cells to ABT-737 by elevating proapoptotic Bim. In striking contrast, increasing Bcl-xL or Bcl-w conferred robust resistance to ABT-737, despite also increasing Bim. Cell-based protein redistribution assays unexpectedly revealed that ABT-737 disrupts Bcl-2/Bim complexes more readily than Bcl-xL/Bim or Bcl-w/Bim complexes. These results have profound implications for how BH3-mimetics induce apoptosis and how the use of these compounds ...
A critical hallmark of tumor cell success is evasion of apoptosis. Mcl-1 or Bcl-2. Finally BH3-M6 sensitizes cells to apoptosis induced from the proteasome inhibitor CEP-1612. Bim Poor Bik Bmf Bet Noxa and Puma) (5). Multi-domain pro-apoptotic protein Bax and Bak are definitely necessary for apoptosis (2). In response to mobile tension they induce the discharge from mitochondria of apoptogenic elements such as for example cytochrome as well as the initiation of intrinsic apoptosis. Nevertheless triggered Bax and Bak still could be kept in balance by binding to anti-apoptotic Bcl-2 protein (8 -10). X-ray diffraction and nuclear magnetic resonance (NMR) research have shown how the amphipathic α-helices of pro-apoptotic protein such as for example Bak or Poor BH3 domains match a hydrophobic pocket shaped from the BH1 BH2 and BH3 domains of Bcl-2 Bcl-XL and Mcl-1 (11). When BH3-just protein bind to anti-apoptotic Bcl-2 protein multi-domain protein Bak or Bax become absolve to induce apoptosis (12). ...
TY - JOUR. T1 - Overexpression of human Bcl-2 in syngeneic rat donor lungs preserves posttransplant function and reduces intragraft caspase activity and interleukin-1β production. AU - Cooke, David T. AU - Hoyt, E. Grant. AU - Robbins, Robert C.. PY - 2005/4/15. Y1 - 2005/4/15. N2 - Background. A significant cause of primary graft failure in lung transplantation is ischemia-reperfusion (I/R). I/R injury generates proinflammatory cytokines, such as interleukin (IL)-1β, and activates the caspase-mediated pathways of alveolar epithelial apoptosis. The authors investigated whether gene transfer of the human antiapoptotic protein Bcl-2 by means of intratracheal adenoviral administration would preserve posttransplant lung function and reduce intragraft activated caspase activity and IL-1β production in syngeneic rat donor lung grafts. Methods. First, 1.0 × 109 plaque-forming units of AdvBcl-2 in phosphate-buffered saline (PBS), AdvNull empty vector in PBS, or PBS alone was administered ...
Purpose: Chronic lymphocytic leukemia cells in lymph nodes (LNs), from which relapses are postulated to originate, display an anti-apoptotic profile in contrast to CLL cells from peripheral blood (PB). The BH3 mimetic ABT-737 antagonizes the anti-apoptotic proteins Bcl-XL and Bcl-2, but not Mcl-1 or Bfl-1. Previously, it was shown that CD40-stimulated CLL cells were resistant to ABT-737. We aimed to define which anti-apoptotic proteins determine resistance to ABT-737 in CLL and whether combination of known anti-leukemia drugs and ABT-737 was able to induce apoptosis of CD40-stimulated CLL cells. Experimental Design: To mimic the LN microenvironment, PB lymphocytes of CLL patients were cultured on feeder cells expressing CD40L and treated with ABT-737 with or without various drugs. In addition, we performed overexpression or knockdown of pro- and anti-apoptotic proteins in immortalized primary B cells. Results: Upon CD40-stimulation patient-specific variations in ABT-737 sensitivity correlated ...
Background:This study was conducted to analyze the frequency, expression patterns, and the impact of individual proteins BCL2, BCL6, and p53 on overall survival (OS) in adult, diffuse large B-cell lymphoma (DLBCL) Patients. BCL2 gene was further investigated for potential alterations at the DNA level and correlated with OS. Materials and Methods: A total of 117 adult well-characterized DLBCL cases were included. The panel of antibodies comprised CD45, CD20, CD79a, CD3, BCL2, BCL6, and p53. PCR was also employed to correlate the events at the DNA level in BCL2. Results: The mean and median ages were 47.74 and 49 with a M:F ratio of 2.07:1. The incidence of BCL2, BCL6, and p53 expression was observed in 64.10%, 37.60%, and 52.13% of cases, respectively. Amplifiable quality DNA was available from 90 cases. BCL2/IGH translocation was found in 35/90 Patients (38.88%) with 24 cases showing BCL2 (MBR)/IGH and 11 cases BCL2 (mcr)/IGH translocation. No association between BCL2 overexpression and BCL2 /IGH
Impaired apoptosis contributes to cancer development and resistance towards chemotherapy, since apoptosis normally eliminates cells with damaged DNA or increased malignant potential. The increased resistance towards cell death often limits therapeutic options in the clinic and is one major problemin current tumor therapy. Different approaches, which have been described so far intend to lower the apoptotic threshold in order to eliminate chemoresistant cancer cells. In the first part of this thesis the anti-tumor potential of the bispecific 4625 oligonucleotide was investigated in combination with chemotherapeutic drugs in vitro and in vivo. The second part describes the anti tumor activity of the recombinant Ep-CAM specific scFv immunotoxin 4D5MOC-B-ETA in vitro and in nude mice. Bcl-2 and Bcl-xL are inhibitors of apoptosis frequently overexpressed in malignant tumor cells. Downregulation of either Bcl-2 or Bcl-xL lowers the apoptotic threshold and tumor cells undergo apoptosis. The 4625 ...
Impaired apoptosis contributes to cancer development and resistance towards chemotherapy, since apoptosis normally eliminates cells with damaged DNA or increased malignant potential. The increased resistance towards cell death often limits therapeutic options in the clinic and is one major problemin current tumor therapy. Different approaches, which have been described so far intend to lower the apoptotic threshold in order to eliminate chemoresistant cancer cells. In the first part of this thesis the anti-tumor potential of the bispecific 4625 oligonucleotide was investigated in combination with chemotherapeutic drugs in vitro and in vivo. The second part describes the anti tumor activity of the recombinant Ep-CAM specific scFv immunotoxin 4D5MOC-B-ETA in vitro and in nude mice. Bcl-2 and Bcl-xL are inhibitors of apoptosis frequently overexpressed in malignant tumor cells. Downregulation of either Bcl-2 or Bcl-xL lowers the apoptotic threshold and tumor cells undergo apoptosis. The 4625 ...
There is an increasing body of evidence demonstrating the implication of apoptosis and/or its regulating proteins in the outcome of tumors treated by RT and chemotherapy (7 , 21, 22, 23, 24, 25) . In the present study, we investigated the value of the expression of the proapoptotic proteins Bax and p53 and of the antiapoptotic proteins Bcl-2 and Mcl-1, as well as the value of spontaneous apoptosis regarding the outcome in patients who have had nonsurgical treatment for anal cancer. With the exception of p53, to our knowledge, this is the first study that addresses the question of prognostic significance of these proteins in this disease. Although rare, anal carcinoma is one of the few cancers treated primarily by RT and chemotherapy. Identification of factors that can reliably predict a favorable treatment outcome would, thus, have paramount clinical importance in this disease. Moreover, biological predictive factors shown to be reliable in anal carcinoma might prove to be of value in other ...
According to biochemical assays, the Bcl-2 protein Diva from mouse regulates programmed cell death by heterodimerizing with other members of the family and by interacting with the apoptotic protease-activating factor Apaf-1. In typical Bcl-2 heterodimers, peptide fragments comprising the Bcl-2 homology domain 3 (BH3 domain) of proapoptotic members are capable of forming functional complexes with prosurvival proteins. High-resolution structural studies have revealed that the BH3 peptide forms an α-helix positioned in a canonical hydrophobic cleft of the antiapoptotic protein. Because Diva shows mutations in conserved residues within this area, it has been proposed to have a different interacting surface. However, we showed previously that Diva binds through the canonical groove the BH3 peptide of the human Bcl-2 killing member Harakiri. To further test Divas binding capabilities, here we show Nuclear Magnetic Resonance (NMR) data, indicating that Diva binds peptides derived from the BH3 domain ...
Functional interaction of Bcl-2/Bcl-xL and Bax/Bak, but not Bid/Bik, with the VDAC. Bax/Bak directly opens the VDAC to induce cytochrome c release, while Bcl-2/
O15519: CASP8 and FADD-like apoptosis regulator; Caspase homolog; CASH; Caspase-eight-related protein; Casper; Caspase-like apoptosis regulatory protein; CLARP; Cellular FLICE-like inhibitory protein; c-FLIP; FADD-like antiapoptotic molecule 1; FLAME-1; Inhibitor of FLICE; I-FLICE; MACH-related inducer of toxicity; MRIT; Usurpin; CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12; ...
Apoptosis is the physiological process used by an organism to selectively eliminate cells that are no longer needed, have been damaged or are dangerous ( Kerr et al., 1972). This process, critical for sculpting organs during development and ensuring homeostasis throughout life, has been conserved during evolution ( Vaux and Strasser, 1996). Defects in the control of apoptosis have been implicated as a cause or a contributing factor in a variety of diseases. For example, abnormal survival of cells that should be killed can cause cancer ( Strasser et al., 1990) or autoimmune disease ( Bouillet et al., 1999; Strasser et al., 1991b; Watanabe-Fukunaga et al., 1992), whereas premature death of normally long-lived cells may be the cause of certain degenerative disorders ( Barr and Tomei, 1994).. Genetic and biochemical studies have identified two major pathways to programmed cell death that are largely independent ( Strasser et al., 1995). On the one hand, apoptosis can be triggered by ligation of a ...
A-371191 is a novel Bcl-XL antagonist. Bcl-XL is one of the anti-apoptotic Bcl-2 family members that plays a key role in the regulation of apoptosis. Overexpression of Bcl-XL occurs in numerous cancers and its overexpression correlates with increased resistance to many chemocytotoxic drugs.
Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity (PubMed:8183370). Interacts with EI24 (By similarity). Also interacts with APAF1, BBC3, BCL2L1, BNIPL, MRPL41 and TP53BP2. Binding to FKBP8 seems to target BCL2 to the mitochondria and probably interferes with the binding of BCL2 to its targets. Interacts with BAG1 in an ATP-dependent manner. Interacts with RAF1 (the Ser-338 and Ser-339 phosphorylated form). Interacts (via the BH4 domain) with EGLN3; the interaction prevents the formation of the BAX-BCL2 complex and inhibits the anti-apoptotic activity of BCL2. Interacts with G0S2; this interaction also prevents the formation of the anti-apoptotic BAX-BCL2 complex. Interacts with RTL10/BOP. Interacts with the SCF(FBXO10) complex. Interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV ...
The Pa-PDT induced p-JNK caused down-regulation of the pro-apoptotic protein bcl-2 that facilitates the collapse of mitochondrial membrane and eventually initiates the intrinsic apoptotic pathway ...
摘要(Abstract): 目的探讨孕期不同剂量苯并(a)芘暴露对仔鼠肝脏凋亡相关蛋白Bcl-xl和Bax表达水平的影响。方法将雌雄大鼠合笼后雌性SD大鼠见阴栓确定为受孕,以检出日为孕期第0 d。将孕鼠随机分为4组,每组8只,分为对照组(玉米油)和苯并(a)芘处理组(0.75 mg/kg、1.5 mg/kg和3 mg/kg)。从妊娠第3 d开始经灌胃苯并(a)芘直到妊娠第17 d结束,分别在孕0、4、7、14、19 d称孕鼠体重。待其自然分娩后24 h内测量仔鼠的体重、身长及尾长,然后取仔鼠肝脏,采用Western blot方法检测仔鼠肝脏中Bcl-xl和Bax蛋白的表达水平。结果随着孕期苯并(a)芘暴露水平的增加,新生仔鼠体重、身长、尾长等生长发育指标均有一定程度的下降,但未达到显著性差异(P>0.05)。Western blot结果显示,与对照组相比,中、高剂量染毒组仔鼠肝脏的Bcl-xl蛋白表达均明显下降,Bax蛋白表达均明显升高,差异均有统计学意义( ...
Venetoclax (ABT-199, GDC-0199)是一种Bcl-2选择性抑制剂,无细胞试验中Ki为<0.01 nM,比作用于Bcl-xL和Bcl-w选择性高4800倍以上,对Mcl-1没有抑制活性。有研究证明 Venetoclax 在三阴性乳腺癌 MDA-MB-231 细胞中诱导细胞生长抑制,凋亡,细胞周期停滞和自噬。Phase 3。
Bak小鼠单克隆抗体[AT8B4](ab104124)可与小鼠, 人样本反应并经WB, ELISA, ICC/IF实验严格验证。中国75%以上现货,所有产品提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
This cell transport lab will give your students a hands-on and up-close view of osmosis, diffusion, and plasmolysis in living cells. This lab has two different activities. In the first part of this lab, the observation of plasmolysis in a living cell is a qualitative measurement.
Purpose: : In the intrinsic apoptotic pathway, Bcl-2 family member protein Bax triggers cytochrome C release from mitochondria. Thus, it leads to an activation of the downstream caspase cascade ultimately resulting in apoptosis. The aim of the study was to investigate kinetics and up-regulation of this central pro-apoptotic factor in human corneal endothelial cells. Methods: : Human corneal endothelial cells (HCECs, 100% confluence) were incubated with the intrinsic apoptotic inducer Etoposide (a topoisomerase II inhibitor) in increasing concentrations (1.25, 2.5, 5.0 µg/ml). Bax protein level was determined within twelve hours using cell-based ELISA. These results were confirmed by Western blot. The rate of apoptotic HCECs was measured 6h, 12h, 24h and 48h after incubation with Etoposide by flow cytometric assay using Annexin V and Propidium Iodide. Results: : We detected a positive correlation between increasing Bax protein level and apoptotic HCECs. Specifically, HCECs showed an early ...
Looking for online definition of Proto-oncogene proteins C-bcl-2 in the Medical Dictionary? Proto-oncogene proteins C-bcl-2 explanation free. What is Proto-oncogene proteins C-bcl-2? Meaning of Proto-oncogene proteins C-bcl-2 medical term. What does Proto-oncogene proteins C-bcl-2 mean?
CCAR1; cell division cycle and apoptosis regulator 1; cell division cycle and apoptosis regulator protein 1; CARP 1; CARP1; FLJ10590; death inducer with SAP domain; cell cycle and apoptosis regulatory protein 1; MGC44628; RP11-437A18.1; novel protein similar to vertebrate cell division cycle and apoptosis regulator 1 (CCAR1 ...