Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
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 Proteins), which controls the migration of head and neck cancer cells, and suggests that ERK3 (show MAPK4 Proteins) 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.
our study demonstrates that USP22 (show USP22 Proteins) is indispensable for gastric cancer stem cell self-renewal through stabilization of BMI1.
elevating the levels of BMI1 regulated miRNAspromoted Mesenchymal to Epithelial transition by regulating the expression of N-Cadherin (show CDH2 Proteins), Vimentin (show VIM Proteins), beta-Catenin (show CTNNB1 Proteins), Zeb, Snail (show SNAI1 Proteins) thereby resulting in decreased invasion, migration and proliferation
BMI-1, TIM-3 (show HAVCR2 Proteins) and CLL-1 (show COLEC10 Proteins) have roles in acute myeloid leukemia (show BCL11A Proteins) prognosis and therapy
miR128-1 could function as a tumor suppressor in glioblastoma multiforme by negatively regulating tumor cell proliferation, invasion and self-renewal through direct targeting BMI1 and E2F3.
these data suggest that Bmi-1 could serve as a novel prognostic biomarker in pediatric primary acute lymphoblastic leukemia (ALL)and may be partially regulated by Sall4a (show SALL4 Proteins). Our study also showed that Bmi-1 could serve as a new therapeutic target for the treatment of pediatric ALL.
The findings indicate that BMI1-mediated IDAX (show CXXC4 Proteins) epigenetic suppression is crucial for enhancement of colon carcinogenesis.
BMI1 and UBR5 repress the polymerase II (Pol II)-mediated transcription at damaged sites
Data suggest BMI1 overexpression as a novel mechanism leading to EphA7 (show EPHA7 Proteins) inactivation via H3K27 trimethylation and DNA methylation (show HELLS Proteins) 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 Proteins), T cell activation, and RANKL (show TNFSF11 Proteins) 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 Proteins) transgene did not enhance tumour progression or drive metastasis formation. In conclusion, we here report the generation of a wildtype Ezh2 (show EZH2 Proteins) overexpression mouse model that allows for intravital surveillance of tissues with activated transgene
BMI1 and MEL18 (show PCGF2 Proteins) 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 (show STAT3 Proteins) in colon epithelial cells.
Data show that C/EBPalpha (show CEBPA Proteins) is a tumor suppressor in lung cancer and that BMI1 is required for the oncogenic process downstream of C/EBPalpha (show CEBPA Proteins) loss.
KLF4 (show KLF4 Proteins) modulates development of BMI1-expressing intestinal stem cell-derived lineage following gamma-radiation-induced gut (show GUSB Proteins) 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 (show CBX2 Proteins) proteins not previously identified in olfactory basal cells are essential for self-renewal.
Bmi1 acts immediately downstream of CCAAT enhancer binding protein-alpha (show CEBPA Proteins) 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 Proteins)' untranslated region (UTR), and a 1,956 bp 3 (show BST1 Proteins)' UTR. The transcript contains no signal peptides and there are no transmembrane regions in the pig Bmi1 coded protein.
This locus represents naturally occurring read-through transcription between the neighboring COMM domain-containing protein 3 and polycomb complex protein BMI-1 genes on chromosome 10. The read-through transcript produces a fusion protein that shares sequence identity with each individual gene product.
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
, COMMD3-BMI1 read-through protein
, Polycomb group RING finger protein 4
, RING finger protein 51
, Polycomb group RING finger protein 4-B
, polycomb complex protein BMI-1-B
, polycomb group RING finger protein 4-B
, oncoprotein BMI-1