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Hic-5 regulates GR binding site selection by a novel mechanism, exploiting gene-specific requirements for chromatin remodeling enzymes to selectively influence DNA occupancy and gene regulation by a transcription factor.
As aging increased, more ARA55 were expressed in PZ stromal cells, leading to more sensitive androgen/androgen receptor (AR (show AR Proteins)) signal pathway, then constituting a more feasible environment to cancer cells.
Hic-5 appears to enhance complex formation between MT1-MMP (show MMP14 Proteins) and FAK (show PTK2 Proteins) in activated endothelial cells, which likely coordinates matrix proteolysis and cell motility.
Hic-5 plays a central role in the positive feedback ROS (show ROS1 Proteins)-JNK (show MAPK8 Proteins) signaling cascade that regulates hepatocellular carcinoma progression.
Hic-5 influences the genomic occupancy of multiple steroid receptors and thereby blocks some aspects of hormonal regulation.
Endothelial Hic-5 plays an important role in the formation of microvilli-like structures and in the interaction between ECs and monocytes, leading to monocyte recruitment and subsequent development of atherosclerosis.
Studies in vitro and in vivo using TGF-beta1 (show TGFB1 Proteins) and TGFB1I1 shRNA demonstrated that TGFB1I1 is required for TGF-beta (show TGFB1 Proteins) stimulated EMT (show ITK Proteins) that contributes to malignant progression of astrocytomas.
Hic-5 siRNA also suppressed TGF-beta2 (show TGFB2 Proteins)-induced fibrogenic activity and dexamethasone-induced myocilin (show MYOC Proteins) expression in HTM cells.
Hic5 coordinates AR signaling with adhesion and extracellular matrix contacts to regulate cell behavior in the tumor microenvironment.
Hic-5 suppresses senescence and profibrotic activities of myofibroblasts by down-regulating Nox4 (show NOX4 Proteins) expression.
paxillin (show PXN Proteins) and Hic-5 have both redundant and distinctive functions in invadosome formation.
Hic-5 deficiency attenuates the activation of hepatic stellate cells and liver fibrosis though reducing the TGF-beta (show TGFB1 Proteins)/Smad2 (show SMAD2 Proteins) signaling by upregulation of Smad7 (show SMAD7 Proteins)
Hic-5 regulates mesangial cell proliferation in proliferative glomerulonephritis in mice.
Hic-5 is a transcription coregulator that acts before and/or after glucocorticoid receptor (show NR3C1 Proteins) genome occupancy in a gene-selective manner.
Hic-5 is expressed in B16-F1 murine melanoma cells.
identified Hic-5 as a novel and specific regulatory factor for thrombin (show F2 Proteins)-induced alphaIIbbeta3 activation and subsequent platelet aggregation in mice.
the HIC-5- and KLF4 (show KLF4 Proteins)-dependent mechanism transactivates p21(Cip1 (show CDKN1A Proteins)) in response to anchorage loss
These data identify discrete roles for paxillin (show PXN Proteins) and Hic-5 in Rac1 and RhoA (show RHOA Proteins)-dependent cell adhesion formation and maturation; processes essential for productive cell migration.
Transforming growth factor-beta1-induced transcript 1 protein, a novel marker for smooth muscle contractile phenotype, is regulated by serum response factor/myocardin protein.
This gene encodes a coactivator of the androgen receptor, a transcription factor which is activated by androgen and has a key role in male sexual differentiation. The encoded protein is thought to regulate androgen receptor activity and may have a role to play in the treatment of prostate cancer. Multiple transcript variants encoding different isoforms have been found for this gene.
transforming growth factor beta 1 induced transcript 1
, androgen receptor coactivator ARA55
, transforming growth factor beta-1-induced transcript 1 protein-like
, androgen receptor coactivator 55 kDa protein
, androgen receptor-associated protein of 55 kDa
, hydrogen peroxide-inducible clone 5 protein
, transforming growth factor beta-1-induced transcript 1 protein
, TGF beta-stimulated clone 5
, androgen receptor activator of 55 kDa