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anti-Human BMI1 Antibodies:
anti-Mouse (Murine) 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
Show all 6 Pubmed References
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
Show all 2 Pubmed References
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
Show all 2 Pubmed References
Human Monoclonal BMI1 Primary Antibody for 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 for 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
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
Show all 3 Pubmed References
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
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 Monoclonal BMI1 Primary Antibody for CyTOF, FACS - ABIN4900505
Shen, Chen, Ding, Qi, Cen, Wang, Yao, Chen: BMI1 reprogrammes histone acetylation and enhances c-fos pathway via directly binding to Zmym3 in malignant myeloid progression. in Journal of cellular and molecular medicine 2014
indicate USP22 (show USP22 Antibodies) as a novel deubiquitinase of BMI1 in glioma
miR (show MLXIP Antibodies)-200c inhibited epithelial-mesenchymal transition by targeting the BMI-1 gene through the phospho-AKT (show AKT1 Antibodies) pathway.
Data indicate that miR (show MLXIP Antibodies)-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 (show HSP90AA2 Antibodies) could positively regulate the self-renewal of BCSCs by facilitating the nuclear translocation of c-Myc (show MYC Antibodies) and EZH2 (show EZH2 Antibodies) 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.
Authors found that compared with control subjects, BMI1 mRNA expression in whole blood of advanced NSCLC patients was decreased. Similarly, authors observed decreased BMI1 mRNA expression in primary tumors compared to normal lungs from operable NSCLC patients.
study revealed a molecular pathway consisting of BMI1, miRNA let-7i, and ERK3 (show MAPK4 Antibodies), which controls the migration of head and neck cancer cells, and suggests that ERK3 (show MAPK4 Antibodies) kinase is a potential new therapeutic target in head and neck cancers, particularly those with BMI1 overexpression.
Study suggests that BMI-1 is involved in the cellular premature senescence of human dental pulp stem cells triggered by oxidative stress.
Findings extend current knowledge of the role of BMI1 and CHD7 (show CHD3 Antibodies) in medulloblastoma pathogenesis, and they raise the possibility that pharmacological targeting of BMI1 or ERK (show EPHB2 Antibodies) may be particularly indicated in a subgroup of MB with low expression levels of CHD7 (show CHD3 Antibodies)
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 (show MLXIP Antibodies)-203 is repressed by EZH2 (show EZH2 Antibodies) in both embryonic and adult neural stem/progenitor cells (NSPCs). MiR (show MLXIP Antibodies)-203 negatively regulates the proliferation of NSPCs. One of PRC1 (show PRC1 Antibodies) components, Bmi1, is a downstream target of miR (show MLXIP Antibodies)-203 in NSPCs.
Data suggest BMI1 overexpression as a novel mechanism leading to EphA7 (show EPHA7 Antibodies) inactivation via H3K27 trimethylation and DNA methylation (show HELLS Antibodies) 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 (show ROS1 Antibodies), T cell activation, and RANKL (show TNFSF11 Antibodies) 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 (show EZH2 Antibodies) transgene did not enhance tumour progression or drive metastasis formation. In conclusion, we here report the generation of a wildtype Ezh2 (show EZH2 Antibodies) overexpression mouse model that allows for intravital surveillance of tissues with activated transgene
BMI1 and MEL18 (show PCGF2 Antibodies) contribute to the development of colitis-associated cancer in mice by promoting proliferation and reducing apoptosis via suppressing expression of Reg3b (show REG3B Antibodies). REG3B (show REG3B Antibodies) negatively regulates cytokine-induced activation of STAT3 (show STAT3 Antibodies) in colon epithelial cells.
Bmi1 acts immediately downstream of CCAAT enhancer binding protein-alpha (show CEBPA Antibodies) to regulate the survival and self-renewal of hematopoietic stem cells and contribute to the erythropoietic dysplasia.
Pig Bmi1 cDNA is 3,193 bp in length and consists of a 981 bp open reading frame, a 256 bp 5 (show HSPD1 Antibodies)' untranslated region (UTR (show UTS2R Antibodies)), and a 1,956 bp 3 (show BST1 Antibodies)' UTR (show UTS2R Antibodies). 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