Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Alle Spezies anzeigen
Weitere Synonyme anzeigen
Wählen Sie die Spezies und Applikation aus
anti-Human BMI1 Antikörper:
anti-Mouse (Murine) BMI1 Antikörper:
anti-Rat (Rattus) BMI1 Antikörper:
Sie gelangen zu unserer vorgefilterten Suche.
Human Monoclonal BMI1 Primary Antibody für 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
Show all 6 Pubmed References
Human Polyclonal BMI1 Primary Antibody für 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 für 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
Show all 4 Pubmed References
Human Monoclonal BMI1 Primary Antibody für 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
Show all 2 Pubmed References
Human Monoclonal BMI1 Primary Antibody für ChIP - ABIN2668619
Lafkas, Rodilla, Huyghe, Mourao, Kiaris, Fre: Notch3 marks clonogenic mammary luminal progenitor cells in vivo. in The Journal of cell biology 2013
Show all 2 Pubmed References
Human Polyclonal BMI1 Primary Antibody für 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
Show all 3 Pubmed References
Human Monoclonal BMI1 Primary Antibody für ELISA, WB - ABIN560071
Andrews, Banting, Damjanov, Arnaud, Avner: Three monoclonal antibodies defining distinct differentiation antigens associated with different high molecular weight polypeptides on the surface of human embryonal carcinoma cells. in Hybridoma 1985
Show all 2 Pubmed References
Human Polyclonal BMI1 Primary Antibody für IF, WB - ABIN541267
Alkema, Wiegant, Raap, Berns, van Lohuizen: Characterization and chromosomal localization of the human proto-oncogene BMI-1. in Human molecular genetics 1994
Show all 3 Pubmed References
Human Polyclonal BMI1 Primary Antibody für ICC, IF - ABIN257760
Ismail, Andrin, McDonald, Hendzel: BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair. in The Journal of cell biology 2010
Human Polyclonal BMI1 Primary Antibody für ICC, IF - ABIN152245
Kang, Qi, Zuo, Wang, Zou, Schwartz, Cheng, Yeh: SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development. in Molecular cell 2010
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.
miR-200c inhibited epithelial-mesenchymal transition by targeting the BMI-1 gene through the phospho-AKT pathway.
Data indicate that miR-203 suppressed BMI1 polycomb ring finger oncogene protein (Bmi-1) expression by directly targeting the 3'-untranslated region.
High BMI-1 expression is associated with invasion, metastasis, and epithelial-to-mesenchymal transition of gastric cancer.
Bmi1 promoted invasion and migration of CD133+Hep G2 cells.
our data suggested that Hsp90alpha could positively regulate the self-renewal of BCSCs by facilitating the nuclear translocation of c-Myc and EZH2 to maintain BMI1 expression.
These preclinical data in mouse models and human cells provide a strong rationale for the development of pharmacological approaches to target BMI1-mediated mitochondrial regulation and protection from DNA damage to sustain the regenerative potential of the skeletal muscle in conditions of chronic muscle wasting.
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
Our work revealed that MOZ and BMI1 regulate HSCs in a synergistic manner by acting on distinct processes required to maintain HSCs.
Bmi-1 played a critical role in the protection from acute tubular necrosis by maintaining mobilization of renal stem cells and would be a novel therapeutic target for preventing the progression of ATN
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