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cytoplasmic LIM protein that binds glial glutamate transporter GLT-1 and is proposed to allow glial glutamate transporter GLT-1 to regulate intracellular signaling or interact with the cytoskeleton. Additionally we are shipping AJUBA Antibodies (23) and many more products for this protein.
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The results in this study uncovered that JUB was a regulator involved in proliferation of glioma cells, and it could be used as a potential therapeutic target for glioma.
AJUBA negatively regulates YAP activity through the LATS family, and inactivation of AJUBA is a novel key mechanism in malignant mesothelioma cell proliferation
the LIM protein JUB serves as a tumor-promoting gene in colorectal cancer by promoting epithelial-mesenchymal transition, a critical process of metastasis.
The LIM (show PDLIM5 Proteins) domain of Ajuba can competitively bind to the N-terminal of Aurora-A (show AURKA Proteins), and inhibited the interaction between N-terminal and C-terminal of Aurora A (show AURKA Proteins).
A Rac-PAK1-Ajuba feedback loop integrates spatiotemporal signaling with actin remodeling at cell-cell contacts and stabilizes preassembled cadherin complexes.
Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors and rexinoid receptor subtypes.
Ajuba contributes to the bridging of the cadherin adhesive complexes to the actin cytoskeleton and as such contribute to the formation or strengthening of cadherin-mediated cell-cell adhesion.
in addition to its effects upon Rac activity, Ajuba can also influence cell migration through regulation of PI(4,5)P2 synthesis through direct activation of PIPKIalpha enzyme activity
Ajuba is a new cytosolic component of the IL-1 signaling pathway modulating IL-1-induced NF-kappaB activation b (show IL1A Proteins)y influencing the assembly and activity of the aPKC/p62/TRAF6 multiprotei (show GTF2H1 Proteins)n sign (show TRAF6 Proteins)aling complex
Ajuba promoted GSK-3beta-mediated phosphorylation of beta-catenin by reinforcing the association between beta-catenin and GSK-3beta.
Ajuba recruits p300/CBP (show CREBBP Proteins) via its LIM (show PDLIM5 Proteins) domain and facilitates p300/CBP (show CREBBP Proteins) binding to PPARg (show PPARG Proteins). Moreover, Ajuba, PPARg (show PPARG Proteins), p300/CBP (show CREBBP Proteins) can cooperatively occupy the PPARg (show PPARG Proteins) target promoters and concomitantly increases histone acetylation at these loci.
Ajuba is a novel coactivator for liver X receptors and may play important role in lipid and glucose metabolism.
Findings support the importance of adhesion molecules (VE-cadherin and CD31), survivin, and Ajuba in modulating the Hippo pathway, which regulates, in part, proliferation and survival in hemangioendotheliomas.
PKD1-mediated phosphorylation of SNAI1 occurs in the nucleus and generates a nuclear, inactive DNA/SNAI1 complex that shows decreased interaction with its co-repressor Ajuba.
This paper presents evidence indicating that the human and mouse Ajuba is a new cytosolic component of the IL-1 (show IL1A Proteins) signaling pathway, influencing the assembly and activity of the aPKC/p62 (show GTF2H1 Proteins)/TRAF6 (show TRAF6 Proteins) multiprotein signaling complex.
identification of the protein arginine methyltransferase 5 (PRMT5 (show PRMT5 Proteins)) as an effector recruited to SNAIL (show SNAI1 Proteins) through an interaction with AJUBA that functions to repress the SNAIL (show SNAI1 Proteins) target gene, E-cadherin (show CDH1 Proteins)
cytoplasmic LIM protein that binds glial glutamate transporter GLT-1 and is proposed to allow glial glutamate transporter GLT-1 to regulate intracellular signaling or interact with the cytoskeleton
LIM domain-containing protein ajuba
, jub, ajuba homolog
, protein ajuba
, Ajuba protein
, ajuba homolog