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anti-Human BMI1 Antibodies:
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Human Monoclonal BMI1 Primary Antibody for BI, IHC (f) - ABIN2688857
Dimri, Martinez, Jacobs, Keblusek, Itahana, Van Lohuizen, Campisi, Wazer, Band: The Bmi-1 oncogene induces telomerase activity and immortalizes human mammary epithelial cells. in Cancer research 2002
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Human Polyclonal BMI1 Primary Antibody for IHC (p), ELISA - ABIN542707
Itahana, Zou, Itahana, Martinez, Beausejour, Jacobs, Van Lohuizen, Band, Campisi, Dimri: Control of the replicative life span of human fibroblasts by p16 and the polycomb protein Bmi-1. in Molecular and cellular biology 2002
Show all 3 Pubmed References
Human Polyclonal BMI1 Primary Antibody for FACS, IF - ABIN652702
Chagraoui, Niessen, Lessard, Girard, Coulombe, Sauvageau, Meloche, Sauvageau: E4F1: a novel candidate factor for mediating BMI1 function in primitive hematopoietic cells. in Genes & development 2006
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Human Monoclonal BMI1 Primary Antibody for ChIP - ABIN2668619
Lafkas, Rodilla, Huyghe, Mourao, Kiaris, Fre: Notch3 marks clonogenic mammary luminal progenitor cells in vivo. in The Journal of cell biology 2013
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Human Monoclonal BMI1 Primary Antibody for ICC, FACS - ABIN968985
Edwards, Witherspoon, Wang, Afrasiabi, Pham, Birnbaumer, Lipkin: Epigenetic repression of DNA mismatch repair by inflammation and hypoxia in inflammatory bowel disease-associated colorectal cancer. in Cancer research 2009
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Human Monoclonal BMI1 Primary Antibody for ICC, IF - ABIN2668620
Bracken, Kleine-Kohlbrecher, Dietrich, Pasini, Gargiulo, Beekman, Theilgaard-Mönch, Minucci, Porse, Marine, Hansen, Helin: The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells. in Genes & development 2007
Human Monoclonal BMI1 Primary Antibody for ChIP, ICC - ABIN4284857
Courel, Friesenhahn, Lees: E2f6 and Bmi1 cooperate in axial skeletal development. in Developmental dynamics : an official publication of the American Association of Anatomists 2008
Human Polyclonal BMI1 Primary Antibody for IHC (fro), WB - ABIN2477677
Mandal, Boitano, Maxwell, Lou, Alexander: Ninety-eight penetrating vascular injuries: a review of a two and one-half year experience. in The Journal of trauma 1976
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Human Polyclonal BMI1 Primary Antibody for IF, WB - ABIN6714435
Zhang, Wang, Huang, Yang, Cai, Zhang, Zhu, Qian, Xu: H. pylori infection-induced MSC differentiation into CAFs promotes epithelial-mesenchymal transition in gastric epithelial cells. in International journal of molecular medicine 2014
Human Polyclonal BMI1 Primary Antibody for ICC, IF - ABIN257760
Ismail, Andrin, McDonald, Hendzel: BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair. in The Journal of cell biology 2010
Data suggest that ascertaining B-cell-specific Mo-MLV insertion site-1 (BMI1) over-expression may be useful in identifying patients who might benefit from therapies directed at reversing the chromatin-modifying functions of BMI1.
TA-III is a potent inhibitor of BMI1.
Bmi1 silencing suppresses cancer stemness in HEC1A and Ishikawa cells.
Fine-mapping at chromosome 10p12 identified rs11591377 variant upstream of BMI1, residing within a hematopoietic stem cell enhancer of BMI1, and which showed significant preferential binding to MYBL2. This variant was found associated with childhood acute lymphoblastic leukemia.
P16INK4a deletion promoted proliferation, reduced senescence and and subsequently inhibited epithelial-mesenchymal transition of Bmi1-knocked-down tubular epithelial cells.
Implementation of micronucleus assay and Bmi-1 expression analysis in blood as possible cytogenetic and molecular biomarkers.
BMI1 binds the androgen receptor (AR) and prevents MDM2-mediated AR protein degradation, resulting in sustained AR signaling in prostate cancer cells.
Findings suggest there might be a relationship between BMI-1 mRNA and protein levels, and clinicopathological characteristics, including NIH risk grade, tumor size as well as infiltration and metastasis, of GIST patients.
Upregulation of BMI1 correlates with advanced stages of breast neoplasm, poor prognosis and resistance to radiation and chemotherapy. BMI1 seems to be a key player in EMT, chemo-resistance and cancer stemness. Studies showed that reduction of BMI protein level in tumor cells results in inhibition of cell proliferation, induction of apoptosis, and increases susceptibility to cytotoxic agents and radiation therapy. [review]
Down-regulating Bmi-1 may inhibit the biological properties of CD133+ LCSC by blocking NF-kappaB signaling pathway, which lays a scientific foundation for the clinical treatment of liver cancer.
BMI1 expression is not associated with Colorectal Cancer.
these findings provide further evidence on the tumor-suppression function of miR-630 in breast cancer, and clarify BMI1 as a novel functional target gene of miR-630.
BMI1 is a potential biomarker in epithelial ovarian cancermanagement, especially for tumor progression and chemo-resistance. Molecular traits, including BMI1 and core genes in Focal adhesion and PI3K/AKT pathways, might be alternatives as therapeutic targets for EOC.
Through radiotherapy and chemotherapy assays, the function of miR-128a on chemoradiotherapy was evaluated. The correlation of miR-128a with BMI1 was identified by performing real-time PCR.
Study demonstrated that BMI-1 was overexpressed in oesophageal squamous cell cancer (ESCC) cells and was related to poor prognosis in ESCC patients. Its knockdown induces radiosensitivity in ESCC and significantly inhibits cell viability, which may contribute to an increased proportion of cells in the G0/G1 phase and cell apoptosis via suppression of the PI3K/Akt signaling pathway.
Interaction of BMI1 with polyhomeotic protein PHC2 and homo-oligomerization via ubiquitin-like domain are necessary for H2A ubiquitination activity of PRC1 and for clonogenic potential of U2OS cells.
ur results reveal that miR-203a may regulate cholesteatoma growth and proliferation by targeting Bmi1. These findings provide insight for the development of novel nonsurgical options for cholesteatoma.
that the down-regulated Bmi-1 might inhibit the proliferation, invasion, and migration of gastrointestinal stromal tumor cells
indicate USP22 as a novel deubiquitinase of BMI1 in glioma
B-lymphoma Moloney murine leukemia virus insertion region-1 promotes self-renewal of radio- and temozolomide-resistant breast cancer cells.
Bmi1 is expressed in the basal epithelium of the central cornea and limbus.
P16INK4a deletion ameliorated renal tubulointerstitial injury in a stress-induced premature senescence model of Bmi1 deficiency.
Bmi1 is a marker for a distinct population of castration-resistant luminal epithelial cells enriched in the proximal prostate that can serve as a cell of origin for prostate cancer
Findings extend current knowledge of the role of BMI1 and CHD7 in medulloblastoma pathogenesis, and they raise the possibility that pharmacological targeting of BMI1 or ERK may be particularly indicated in a subgroup of MB with low expression levels of CHD7
Many Bmi1-positive cells within the tongue cancer specimens failed to proliferate.
High Expressions of BMI1 is associated with breast cancer.
of Bmi1 in lymphocytes can stimulate osteogenesis in vivo and partially rescue defects in skeletal growth and osteogenesis.
miR-203 is repressed by EZH2 in both embryonic and adult neural stem/progenitor cells (NSPCs). MiR-203 negatively regulates the proliferation of NSPCs. One of PRC1 components, Bmi1, is a downstream target of miR-203 in NSPCs.
Data suggest BMI1 overexpression as a novel mechanism leading to EphA7 inactivation via H3K27 trimethylation and DNA methylation by which BMI-1 controls cell proliferation in the postnatal lateral ventricle wall.
Bmi1 plays an important role in regulating the proliferation of cochlear supporting cells.
Results from this study indicate that estrogen deficiency downregulates BMI-1 and subsequently increases ROS, T cell activation, and RANKL production in T cells, thus enhancing osteoclastogenesis and accelerating bone loss.
ompounding a previously described Bmi1-transgene and Pten-deficiency prostate cancer mouse model with the Ezh2 transgene did not enhance tumour progression or drive metastasis formation. In conclusion, we here report the generation of a wildtype Ezh2 overexpression mouse model that allows for intravital surveillance of tissues with activated transgene
BMI1 and MEL18 contribute to the development of colitis-associated cancer in mice by promoting proliferation and reducing apoptosis via suppressing expression of Reg3b. REG3B negatively regulates cytokine-induced activation of STAT3 in colon epithelial cells.
Data show that C/EBPalpha is a tumor suppressor in lung cancer and that BMI1 is required for the oncogenic process downstream of C/EBPalpha loss.
KLF4 modulates development of BMI1-expressing intestinal stem cell-derived lineage following gamma-radiation-induced gut injury in mice.
The retinal phenotype of Bmi1(-/-) mice was characterized by loss of heterochromatin, activation of tandem repeats, oxidative stress and Rip3-associated necroptosis.
Loss of BMI1 enhanced ribonuclease activity of polynucleotide phosphorylase and reduced mtRNA stability
Inducible fate mapping demonstrates that BMI1 is expressed in vivo by multipotent Olfactory epithelium progenitors. expression of BMI1 and other Polycomb proteins not previously identified in olfactory basal cells are essential for self-renewal.
We conclude that silencing of Bmi1 by miR-27b relieves repression of the presynaptic transcriptome and supports neurotransmission in cortical networks.
a full complement of Bmi-1 is required for the intestinal proliferative effects of GLP-2 in both the physiological and pathological setting
Bmi1 acts immediately downstream of CCAAT enhancer binding protein-alpha to regulate the survival and self-renewal of hematopoietic stem cells and contribute to the erythropoietic dysplasia.
10 genes were down-regulated following treatment of the T-ALL cells with 0.15 and 1.5 microg/mL of metal ores at 72 h. Cell growth maintenance, segment specification.
Pig Bmi1 cDNA is 3,193 bp in length and consists of a 981 bp open reading frame, a 256 bp 5' untranslated region (UTR), and a 1,956 bp 3' UTR. The transcript contains no signal peptides and there are no transmembrane regions in the pig Bmi1 coded protein.
Component of a Polycomb group (PcG) multiprotein PRC1- like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones\; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2 (By similarity).
B lymphoma Mo-MLV insertion region 1 homolog
, murine leukemia viral (bmi-1) oncogene homolog
, polycomb complex protein BMI-1
, polycomb group RING finger protein 4
, polycomb group protein Bmi1
, ring finger protein 51
, BMI1 polycomb ring finger oncogene
, B lymphoma Mo-MLV insertion region 1
, polycomb group ring finger 4
, polycomb complex protein BMI-1-A
, polycomb group RING finger protein 4-A
, B lymphoma Mo-MLV insertion region
, Polycomb group RING finger protein 4-B
, polycomb complex protein BMI-1-B
, polycomb group RING finger protein 4-B
, oncoprotein BMI-1