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anti-Human BCL2L10 Anticorps:
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Human Polyclonal BCL2L10 Primary Antibody pour IF, WB - ABIN541211
Ke, Godzik, Reed: Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak. dans The Journal of biological chemistry 2001
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Human Polyclonal BCL2L10 Primary Antibody pour ELISA, WB - ABIN1327714
Guillemin, Lalle, Gillet, Guerin, Hamamah, Aouacheria: Oocytes and early embryos selectively express the survival factor BCL2L10. dans Journal of molecular medicine (Berlin, Germany) 2009
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Human Polyclonal BCL2L10 Primary Antibody pour WB - ABIN223374
Guérin, Cornut-Thibaut, Giscard-Destaing, Pouvreau, Guillemin, Aouacheria: Subcellular dynamics of the maternal cell death regulator BCL2L10 in human preimplantation embryos. dans Human reproduction (Oxford, England) 2013
BCL2L10 (Nrh protein) is localized to the endoplasmic reticulum and is a poor prognostic marker linked with chemotherapy resistance in breast cancer.
marrow BCL2L10 positive cells may be a biomarker for azacitidine response and OS, with a potential impact in clinical practice.
These results suggest that by inhibiting Bcl2l10 activity and promoting contact between endoplasmic reticulum and mitochondria, IRBIT facilitates massive Ca(2+) transfer to mitochondria and promotes apoptosis.
we describe the identification of a structural genetic variant segregating with affective psychosis in a family with multiple members suffering from bipolar I disorder. Using whole-genome sequencing, we delineated the translocation breakpoints as corresponding intragenic events disrupting BCL2L10 and PNLDC1. These data warrant further consideration for BCL2L10 and PNLDC1 as novel candidates for affective psychosis.
Results found that BCL2L10 was down-regulated in human hepatocellular carcinoma (HCC) tissues; its overexpression suppresses cell growth and migration of HCC cell lines. These results suggested that BCL2L10 functions as a tumor-suppressor in HCC.
BCLB expression was a starvation stress sensor inducing apoptosis and autophagy simultaneously in HCC cells through the adenosine monophosphate-activated protein kinase AMPK-mTOR signaling cascade.
Identification of a variant in the BCL2L10 gene as a protective factor for the development of therapy-related myeloid neoplasms and de novo myelodysplastic syndrome.
polyubiquitination and proteasomal turnover dictate the expression level and anti-apoptotic capacity of Bcl-B
Data suggest that BCL2L10 is localized predominantly to mitochondria in high-quality preimplantation embryos/blastocysts; in contrast, abnormal embryos/blastocysts exhibit extra-mitochondrial localization (cytoplasm/cell nucleus) of BCL2L10.
Bcl-B in complex with the BH3 motif of Bim protected cells from Bax-dependent apoptotic pathways.
Bcl-B interacts with the BH3 domain of BECN1 and Bcl-B overexpression reduces autophagy triggered by a variety of pro-autophagic stimuli.
expression is predictive of azacitidine-resistance in myelodysplastic syndrome patients
Ubqln stabilizes BCLb protein, while also promoting monoubiquitination on multiple lysine residues and relocation to the cytosol.
BCL2L10 methylation is associated with myelodysplastic syndromes.
Loss of BCL2L10 protein expression predicts poor clinical outcome in gastric carcinoma.
The apoptotic gene BCL2L10 is a frequent target for aberrant promoter methylation in patients with acute leukemia, de novo and therapy-related.
The pro-apoptotic effect of BCL2L10 and growth promotion by BCL2L10 siRNA in gastric cancer cells suggest that it may be a tumour suppressor.
study evaluates 3D structure of Bcl-2L10 protein using homology modeling and aims to understand plausible functional and binding interactions between Bcl-2L10 with BH3 domain of BAX using protein - protein docking
BCL2L10 is frequently silenced by promoter hypermethylation in gastric cancer.
Thus, these results indicate the existence of a previously undiscovered mechanism by which NM23-H2 involves in the regulation of Diva-mediated apoptosis.
The knockdown of BCL-B resulted in increased apoptosis and mitophagy in hepatic stellate cells, while the overexpression of BCL-B caused the opposite effects.
role for Bcl-B in B cell proliferation and plasmocyte differentiation through its ability to impair B cell death and drive multiple myeloma progression.
Bcl2l10, Tpx2, and Aurka co-localized on the meiotic spindles, and Bcl2l10 was present in the same complex with Tpx2.
Protein-protein interactions involving apoptosis regulator Diva (Boo) and the BH3 domain of proapoptotic Bcl-2 members.
analysis of a novel interaction between Bcl-2 members Diva and Harakiri
Structure and sequence alignment of mouse pro-survival Bcl-2 family members reveals Boo/Diva as a divergent Bcl-2 protein.
The role of Bcl2l10 is strongly associated with oocyte maturation, especially at the MI-MII transition.
BCL2L10 is a novel and prime candidate related to oocyte maturation, fertility, and embryo developmental competence
Nrz phosphorylation is necessary for the generation of IP3-mediated Ca2+ transients and the formation of circumferential actin-myosin cables required for epiboly.
In the yolk syncytial layer, Nrz appears to prevent the release of Ca(2+) from the endoplasmic reticulum by directly interacting with the IP3R1 Ca(2+) channel.
data suggest that Nrz, in addition to its effect on apoptosis, contributes to cell movements during gastrulation by negatively regulating the expression of Snail-1, a transcription factor that controls cell adhesion
The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains conserved BH4, BH1 and BH2 domains. This protein can interact with other members of BCL-2 protein family including BCL2, BCL2L1/BCL-X(L), and BAX. Overexpression of this gene has been shown to suppress cell apoptosis possibly through the prevention of cytochrome C release from the mitochondria, and thus activating caspase-3 activation. The mouse counterpart of this protein is found to interact with Apaf1 and forms a protein complex with Caspase 9, which suggests the involvement of this protein in APAF1 and CASPASE 9 related apoptotic pathway.
anti-apoptotic protein NrH
, apoptosis regulator Bcl-B
, bcl-2-like protein 10
, anti-apoptotic protein Boo
, bcl-2 homolog Diva