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Transcription factor involved in regulating gene activity following the primary growth factor response. Additionally we are shipping JUNB Antibodies (255) and JUNB Kits (9) and many more products for this protein.
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JunB is a regulator of tail organization possibly through integration of several morphogen (show SHH Proteins) signaling pathways.
VEGF (show VEGFA Proteins)-induced endothelial migration is mediated primarily by induction of JunB whereas the promotion of endothelial proliferation by VEGF (show VEGFA Proteins) is mediated by JunB-independent AP-1 (show FOSB Proteins) family members.
Results suggested that JunB could play an important role in promoting cell invasion, migration and distant metastasis in head and neck squamous cell carcinoma via pathways other than epithelial-to-mesenchymal transition.
Highly recurrent mutation of JUNB is associated with nodular lymphocyte predominant Hodgkin lymphoma.
ETS2 (show ETS2 Proteins), HNF4A (show HNF4A Proteins) and JUNB are synergistic master regulators of epithelial-to-mesenchymal transition in cancer.
CARMA1 (show CARD11 Proteins)- and MyD88 (show MYD88 Proteins)-dependent activation of Jun (show JUN Proteins)/ATF-type AP-1 (show FOSB Proteins) complexes is a hallmark of ABC (show ABCB6 Proteins) diffuse large B-cell lymphomas.
PDK1 (show PDK1 Proteins) functions as a tumor promoter in human gallbladder cancer by upregulating JunB, promoting epithelial mesenchymal transformation, and cell migration.
Our findings demonstrate that miRNA-149* may serve as an oncogenic regulator in T-cell acute lymphoblastic leukemia by negatively regulating JunB
The MAPK (show MAPK1 Proteins) pathway plays a primary role in the control of JUNB gene expression.
JunB is likely to be a key target of c-Abl (show ABL1 Proteins) in expression of p21 (show CDKN1A Proteins) in Adriamycin-induced DDR (show DDR1 Proteins).
Caveolin 2 (show CAV2 Proteins) disengages repressed Egr-1 (show EGR1 Proteins) and JunB promoters from lamin A/C (show LMNA Proteins) through disassembly of H3K9me3 in the inner nuclear membrane.
The present data indicate that bovine dialyzable leukocyte extract can block the AP-1 (show JUN Proteins) DNA-binding activity and expression of several transcriptions factors in breast cancer cells.
Data demonstrate for the first time an essential role of JunB-CBFbeta (show CBFB Proteins) signaling for maintaining sarcomere architecture and function.
JUNB is a significant modulator of both classical and alternative macrophage activation.
Study shows that myeloid deletion of JUNB dampens immune polarization and reshapes disease outcomes during infection with both P. berghei and N. brasiliensis by limiting type 1 and type 2 responses, respectively. Thus, JUNB is an important regulator of myeloid responses to both type 1 and type 2 infections in vivo.
Loss of JunB expression led to increased proliferation and decreased senescence, likely owing to decreased p16(Ink4a) and p21(CIP1 (show CDKN1A Proteins)) in epithelial cells.
JunB and c-Jun (show JUN Proteins) expression in post-mitotic oligodendrocytes is mostly dispensable for the maintainance of white matter tracts throughout adult life, even under demyelinating conditions.
JunB controls epidermal growth, barrier formation, and proinflammatory responses through direct and indirect mechanisms, pinpointing SQSTM1 (show SQSTM1 Proteins) as a key mediator of JunB suppression of NF-kappaB (show NFKB1 Proteins)-dependent inflammation
our results suggest a functional cooperation between NFAT1 (show NFAT1 Proteins) and JunB in mediating IL-31 (show IL31 Proteins) gene expression in CD4 (show CD4 Proteins)(+) T cells
an important role of the A2B (show ADORA2B Proteins) receptor-dependent upregulation of JunB in VEGF (show VEGFA Proteins) production and possibly other AP-1 (show JUN Proteins)-regulated events.
In experimental hepatitis, the absence of JUNB in immune cells decreased IFN-gamma (show IFNG Proteins) expression and secretion from NK & NKT (show CTSL1 Proteins) cells, leading to reduced STAT1 (show STAT1 Proteins) pathway activation.
The results show that the junb gene is organized in a nuclear chromatin loop bringing into close spatial proximity the upstream promoter region and the downstream enhancer and that this configuration permits immediate RNA Pol II (show POLR2F Proteins) release on the junb body on binding of LPS (show TLR4 Proteins)-activated NF-kappaB (show NFKB1 Proteins) to the enhancer.
Data indicate that the C-terminal JunB caspase (show CASP3 Proteins) cleavage product functions as a potent inhibitor of AP-1 (show JUN Proteins)-dependent transcription.
Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGATCA-3'.
jun B proto-oncogene
, jun-B proto-oncogene
, activator protein 1
, transcription factor jun-B
, Jun-B oncogene